An Interview about Ilona Banga: Vitamin C, Muscles, and Elastase

Apr 21, 2021 by

Research is my life motif, and it gives me fulfillment.”

— Ilona Banga

Michael F. Shaughnessy

1) Often, her name is noted as Banga Ilona- but where was she born and when?

The native form of this scientist’s name is Banga Ilona. This book uses Western name order. Ilona Banga was born on February 3, 1906, in Hódmezővásárhely, a town situated in the southeastern region of Hungary.

Banga married József Mátyás Baló, a pathologist, in Szeged in 1945. The conscientious couple worked meticulously on research related to arteriosclerosis until he died in 1979. The couple had one son, Mátyás Jr., who became an academic dermatologist. Banga died in Budapest on March 11, 1998.

2) Her early education- where did she go to school, and what were her interests?

Banga considered pursuing a health-related profession but opted as a substitute to study chemistry because her mother did not believe a medical doctor was an appropriate career for a woman.

It was at the University of Szeged in the Southern Great Plain of Csongrád County in Hungary, where she began her higher education studies. After Szeged, Banga continued her education at the University of Vienna and obtained a master’s degree from the University of Debrecen in 1929; her emphasis was chemistry. It was at the University of Debrecen where Banga planned and performed Physiology research under Professor Fritz Verzár.

Following graduation, she became a research assistant in the laboratory of Albert Szent-Györgyi at the University of Szeged’s Institute for Medicinal Chemistry, Figure 1. Banga was this future Nobel laureate’s first associate. She worked with Szent-Györgyi for roughly fifteen years, resulting in twenty-five collaborative publications; however, WWII hindered the extensive circulation of their findings. Szent-Györgyi was pressed into hiding because he was wanted due to his anti-Nazi activities. This dilemma left Banga to safeguard the lab and all its essential research equipment; she posted notices, which were written in German, Russian, and Hungarian, on the door of the Institute of Chemistry disclosing it was researching infectious materials and providing sample drop-off hours. This tactic effectively discouraged anyone who wanted to take their equipment, and the Institute for Medicinal Chemistry persisted undamaged. It was the only institute at the university to not have its facilities or equipment impaired. This act of bravery on Banga’s part was the main reason why the potential looters, the retreating Germans, and the invading Russians stayed clear of the labs and their equipment.


Figure 1. Albert Szent-Györgyi and Ilona Banga in the laboratory.

Later, Banga spent time working out of Liege, Belgium, and Oxford, England. While in Oxford, she studied vitamin B1 with another future Nobel laureate, Severo Ochoa. In the Ochoa lab, Banga finely ground the brains of pigeons, placed them in a buffer solution, and discovered that vitamin B1 pyrophosphate was the active principle of vitamin B1 when an enzyme called cocarboxylase oxidized a central metabolite called pyruvate. Banga also generated the data supporting the conclusion that specific Krebs cycle intermediates like succinate, malate, and fumarate (known as C4 dicarboxylic acids) turned on the pyruvate oxidation process in the pigeon brains. They also found that additional components were necessary for pyruvate oxidation. For instance, they showed that adenylic acid and phosphate were necessary for the biochemical reaction to proceed. Since then, the cocarboxylase enzyme has become well known as pyruvate dehydrogenase, and vitamin B1 is now called thiamine pyrophosphate (TPP). The pyruvate dehydrogenase catalyzes the conversion of pyruvate to acetyl-CoA using a variety of co-factors, such as TPP, nicotinamide adenine dinucleotide (now known as NAD+), flavin adenine dinucleotide (FAD), coenzyme A, and α-lipoic acid. Presumably, Banga and Ochoa’s adenylic acids were NAD+ and FAD. In modern times, this central biochemical reaction is highly regulated.

In 1945, Albert Szent-Györgyi relocated his lab from Szeged to Budapest and Banga joined him there. After some time, she became chief of the Chemical Laboratory of the First Institute of Pathological Anatomy in Budapest, where she studied arteriosclerosis and aging with her husband, József Baló. She retired in 1970. After retiring, she remained involved in the scientific community, serving as a scientific advisor to the Gerontology Institute from 1971 to 1986. As soon as Szent-Györgyi left Hungary for the United States after WWII, Banga stayed and secured the chief of the Chemical Laboratory of the First Institute of Pathological Anatomy in Budapest. She worked alongside her husband, pathologist József Baló, studying arteriosclerosis and transformations to veins during aging in this new position. They discovered the first elastase, an enzyme capable of degrading elastin fibers like those in the vein through this works. Other scientists were at first cynical, but Banga was able to crystallize elastase and satisfy them.

Ilona Banga and Brúnó F. Straub had very different but successful later careers. Banga pursued scientific research throughout her life. In joint research with her husband József Baló on arteriosclerosis, she studied the origin of fiber degradation in vein walls, which led them to discover the enzyme elastase produced by the pancreas (Balo and Banga 1949). Banga thus made exceptional contributions to three different areas; vitamin C and fumarate research (Nobel Prize awarded to Szent-Györgyi), muscle contraction (Szent-Györgyi nomination for a Nobel Prize), and arteriosclerosis research. At the age of 34, in 1940, she became the first female associate professor at the University of Szeged; in 1955, she earned the degree of the Doctor of Sciences.

Banga published more than 60 papers during the years spanning 1948-1965. Banga was the first female associate professor at the university, but she was never promoted to full professor even though (in 1950) Banga received her DSc degree, making her eligible. However, she was the first woman to achieve the rank of Privatdozent (comparable to associate professor) at the University of Szeged (1940). Banga did win prestigious awards, including the Kossuth Prize and the 1st Szent-Györgyi Prize. She wrote two scientific texts, including Structure and Function of Elastin and Collagen, and was a founding fellow of the Hungarian Biochemical Society.

3) Vitamin C—we all know about it—ascorbic acid—But what did she have to do with Vitamin C?

As we mentioned above, Ilona Banga was a key figure involved with the historical discovery of vitamin C in the laboratory of Prof. Albert Szent-Györgyi. Banga and Szent-Györgyi had isolated vitamin C from large amounts of a red pepper spice called paprika of the scientific name Capsicum annuum, Figure 2. The first laboratory isolation of vitamin C was of extreme scientific importance. The laboratory’s chief, Szent-Györgyi, would garner the 1937 medicine or physiology Nobel Prize, in part, for its discovery.

File:Capsicum annuum var. Fiesta - MHNT.jpg

Figure 2. Capsicum annuum var. Fiesta.

As you know, vitamin C is a necessary small molecule for the proper biological functioning of our cells. Humans do not have the cellular machinery to make vitamin C. The tiny molecule must, therefore, be acquired in our diet. According to mariner lore, British sailors and pirates who went on long ocean voyagers took with them an ample supply of limes and sauerkraut, both staples of which contained concentrated amounts of vitamin C. These citrus and fermented foods helped to prevent a severe condition called scurvy, an ailment due to a lack of dietary vitamin C.

A deficiency in vitamin C intake produces the dreaded scurvy, called scorbutus. The seriousness of the scorbutus cannot be overstated. At first, the scurvy patient suffers from extreme fatigue, loss of appetite, fever, nausea, malaise (discomfort and uneasiness), diarrhea, joint & muscle pain, and experienced tiny patches of bleeding from the skin, which is a condition called petechia.

Then, the scurvy can take a turn for the worse, progressing onto more severe and debilitating consequences. Without added vitamin C in a scurvy patient’s diet at this point, he or she would then undergo teeth loosening, bulging eyes, bleeding gums, hair loss, severely affected skin, and bleeding from the joints and muscles. Prolonged scurvy can result in premature curtailment of bone growth in young patients.

In modern days, the scourge of scorbutus has waned, thanks to the pioneering efforts of Banga and Szent-Györgyi, who discovered vitamin C. Scurvy is an infrequent occurrence as foods are fortified with the vital agent, and daily supplements provide an ample amount of ascorbic acid. The present diminishment of scurvy has its origins in the work of Banga and Szent-Györgyi. Banga was a laboratory assistant in Szent-Györgyi’s laboratory at the Institute of Medical Chemistry. They isolated vitamin C from Hungarian pepper, commonly used for paprika, a food spice called Capsicum annuum, a cash crop cultivated in the plains of Hungary near the University of Szeged, Figure 3. The purification of vitamin C was a laborious process. The extraction involved using caustic chemicals and many labor-intensive steps, any one of which could easily ruin the vitamin C if not performed correctly.

Paprika, Capsicum Annuum, Tomato Pepper, Red, Spicy

Figure 3. Capsicum annuum (paprika).

In the laboratory, Banga and Szent-Györgyi acquired large amounts of ripe pepper and destemmed the plants, taking out the seeds and the core but keeping the fleshly fruit, which they found was laden with the vitamin C. Every batch preparation took the form of about 450 liters of the Capsicum plant pulp. Banga and Szent-Györgyi added water and a series of chemicals, like lead acetate and formic acid. Next, they minced the pulp solution and pressed it using a standard fruit press, which produced a large amount of paprika pepper juice.

The next day, Banga and Szent-Györgyi used heat to add more of the lead acetate and formic acid cocktail. Once the pulp was back in a juice solution, they slowly added an ammonia solution in minute amounts until their pulp juice turned into a slightly alkaline character. To achieve the desired pH, they used a chemical titration method. One chemical color indicator called phenolphthalein turns a light pink color when a solution begins to turn alkaline. They also used bromothymol blue that turns yellow or red under high or low pH values, respectively.

Next, Banga and Szent-Györgyi spun the alkaline pulp juice in a high-speed centrifuge, and from the bottoms of the centrifuge tubes, they collected a solid material. They called the solid substance a lead precipitate. They added a little bit of water and a concentrated hydrochloric acid solution to this precipitate, causing the bromothymol blue to turn a red color. After the water is added and the acidic juice is centrifuged again, the material is cooled, turning it into a syrup-like consistency. Under a vacuum, they heated and distilled the syrup, turning it brown.

Banga and Szent-Györgyi then conducted a series of labor-intensive phase extractions by adding an anhydrous acetone solution to their brown syrup, shaking the mixture vigorously, allowing the phases to separate into two layers, and pouring the top oily layer into a separate vessel, leaving behind an acetone bottom layer. They repeated this same phase extraction process four times. From each step, they combined the various acetone layers, which contained the vitamin C. Next, they performed another phase extraction, except they used pure alcohol instead of acetone, plus heat-distilling the alcohol-vitamin C mixture to obtain an alcohol-free vitamin C solution. They repeated the acetone phase extractions all over again to acquire more syrup with concentrated vitamin C. The process was arduous work.

From this highly concentrated vitamin C syrupy liquid, they tried three utterly different purification protocols to acquire vitamin C in a pure state. They tried the so-called acetone method, acid-lead method, or the alkali method, and they found that all three protocols worked to prepare pure vitamin C, Figure 4. When Banga and Szent-Györgyi wrote their paper describing their process, they conveyed that their acetone protocol was the simplest one to perform.

To prepare a pure crystalline state for analyses of biological function, they performed another set of protocols. In their paper, Banga and Szent-Györgyi described this final process as “very tedious” because their starting material was a thick, sticky, and viscous “mother-liquor” substance. Their attempts to finish the purification process were plagued with an enormous loss of purity. At this point, they cut their losses, stating that this last crystallization method needed “improvement.”

File:Vitamine C.png

Figure 4. Vitamin C (ascorbate) structure

Nevertheless, the vitamin C isolation and purification work were enough to get Szent-Györgyi a nomination for the Nobel Prize. His work with Krebs cycle intermediates was the second reason for his nomination. For Banga, there would be no such nomination or accolade forthcoming. These omissions were probably due to her low-level laboratory assistant status rather than as laboratory head, like that for Szent-Györgyi, an established investigator.

4) Our ability to move muscles—we move them daily and rarely think about it—but what is going on inside those muscles—and what did this biochemist have to do with muscles?

Banga and Szent-Györgyi won extensive scientific acclaim after publishing their vitamin C discovery in January of 1934. Along with Szent-Györgyi’s Nobel nomination, Banga received numerous invitations to work in laboratories worldwide. Banga’s first experience with muscle studies began in 1939 when she was a principal investigator working in Szent-Györgyi’s laboratory. Banga and Szent-Györgyi had become intrigued with a new finding reported by a Russian wife and husband team Militza Ljubimova and Vladimir Engelhardt. In the scientific journal called Nature, they reported that muscle contraction involved a protein called myosin and that it might directly split ATP to release the needed energy. If accurate, the work of Ljubimova and Engelhardt predicted the presence of an enzyme called ATPase, which would do the work of splitting ATP so that myosin protein in muscle could perform the contraction.

Banga and Szent-Györgyi decided to enter the field of muscle protein chemistry and repeat the ATPase findings of Ljubimova and Engelhardt. They quickly confirmed the validity of the Russian experiments, which had suggested that ATPase was a part of the myosin protein. Banga and Szent-Györgyi also found that calcium could turn on the ATP splitting action in muscle. They isolated the myosin protein from the muscle of rabbits. Banga and Szent-Györgyi removed the muscle tissues from laboratory animals, boiled the dispersed muscles in hydrochloric acid, and precipitated a muscle protein extract.

They studied the biochemistry of their muscular protein substance. First, Banga and Szent-Györgyi found that the muscle protein material contained ATP and phosphorous. Szent-Györgyi’s laboratory learned that the muscle extract contained the myosin protein and connected to another protein, now called actin. However, they had referred to it as myosin B and their original one as myosin A. In today’s parlance, we understand them to be myosin (formerly myosin A), actin (was myosin B), and the complex of the two as actomyosin. Here, Banga and Szent-Györgyi used a concentrated solution of potassium chloride to produce a sticky muscle extract. They found that the new stickiness was due to the involvement of the actin protein.

Next, Banga had conducted a series of experiments to characterize the muscle protein biochemistry further. Working in Szent-Györgyi’s lab, Banga discovered that the ATP of the muscle proteins lost a chemical group called an amine. The nitrogen of the amine took the form of NH2 ammonia. The amine loss is called deamination, and Banga learned that the ATP deamination occurred if myosin was present. Banga had found that the myosin protein was the culprit responsible for the ATP deamination in the muscle tissue. Following up on this new finding, Banga discovered that ADP lost a phosphate molecule in the muscle extract, a process called dephosphorylation.

Banga also determined that ADP was deaminated, losing an amine group. It seems that Banga was responsible for establishing the fact that ADP deamination always accompanied dephosphorylation. Banga found that myosin was inactivated by removing actin. She did this myosin inhibition by placing her muscle extract in a concentrated potassium chloride solution in a buffer and storing the mixture at room temperature in the lab for two days. This experimental method permitted Banga to perform her phosphatase testing, a technique for measuring dephosphorylation. All of this new muscle protein biochemistry conducted by Banga set the stage for a discovery that Szent-Györgyi himself would later describe as “the most thrilling moment” of his life!

When myosin was placed in a test tube by itself, it did not contract. It was supposed to be the muscle-contracting agent of the tissue. Thinking that actin protein was needed to make the myosin act like a contracting muscle, a thread was prepared, which consisted of myosin and actin. The complex of actin and myosin would be called actomyosin, and to it, they added boiled muscle juice. What they saw next would be the stuff of biochemistry legend. The makeshift thread of actomyosin contracted like a muscle! The material was composed of relatively purified myosin, actin, and ATP plus calcium, supplied by the muscle juice. They had reproduced in the laboratory an ancient behavior committed by living material, namely, movement or motion of a muscle, but outside of a living being! Thanks to the pioneering studies of Banga, they were able to supply the ATP and ions, like calcium, from muscle juice and conduct one of biochemistry’s most thrilling experiments: a muscle contracting outside of its body!

5) Arteriosclerosis—what did she have to do with this very nasty word—that causes all of us such consternation?

Banga and her husband, József Baló, collaborated on research dealing with arteriosclerosis. In 1953, Banga and Baló studied patients with arteriosclerosis. In particular, they measured the amounts of elastase enzyme in the pancreases from patients who died from arteriosclerosis and compared them with the enzyme amounts of people who died from other diseases and in healthy individuals who had died from accidents. They found that healthy people who died from accidents and diseases other than arteriosclerosis had more pancreatic elastase than people who died from arteriosclerosis.

The condition in humans is characterized by a stiffening behavior of the blood vessels, such as the arteries. Arteriosclerosis can differ from atherosclerosis, which is a particular form of arteriosclerosis. Atherosclerosis can affect the arteries by forming a buildup of fats and cholesterol, causing the development of arterial plaques, which then impede the regular flow of blood, Figure 5.


Figure 5. The buildup of lipids (fat) in the artery prevents blood from flowing.

Typically, arteries carry oxygenated blood from the lungs to the tissues, where they help keep cells alive. When a beating heart pumps blood into healthy blood vessels, they can stretch because the artery walls are sort of elastic in their nature. Such arterial elasticity enables the vessels to expand and relieve the higher pressure for smaller vessels downstream in the blood circulation system. When the heart relaxes after its beat, the elastic blood vessels can spring back to their original pre-stretched state to keep the blood pressure at an average level and avoid a dangerous drop in pressure between each of the heartbeats. Thus, the blood vessel elasticity allows the blood to continue flowing to the tissues where blood is needed to supply oxygen.

On the other hand, stiffened or thickened arteries cannot withstand the pressures of the blood fluid as it travels through the vessels. These abnormally stiff arteries can be made less elastic due to calcification. Hardened arteries are less compliant in their ability to stretch when trying to accommodate blood flow from a pumping heart. Thus, the stiffened arteries can increase the so-called stroke volume pressure as blood is pumped into these noncompliant, less-elastic arteries. This enhanced aortic pulse pressure is a pathological process and can result from aging and arteriosclerosis. Such individuals can be at a greater risk for stroke, heart attack, and death.

Banga is widely credited for her discovery of pancreatic elastase. It was the first elastase enzyme ever to be discovered, and it was Banga who found it. Elastase and elastin have since become greatly important in the field of protein biochemistry.

Banga’s pancreatic elastase has relevance in the digestive breakdown of proteins. Elastase serves as a good model protein for mechanistic studies of degradative proteinase activities. Today, elastase is often grouped with other famous hydrolytic enzymes, like trypsin and chymotrypsin. The three enzymes all work by using the serine protease mechanism. In recent years, it has been found that the elastase enzymes that directly function in the blood vessels come from specialized macrophages. In 2008, a study showed that atherosclerotic plaques harbor elastase made by inflammatory cells, like neutrophils. It is thought that the extracellular matrix material degrades and becomes weakened, contributing to the pathology of arteriosclerosis.

6) Banga and her husband discovered “the first elastase.” What exactly is this, and why is it important?

Banga and József Baló were married in 1945. They began their collaboration in 1947 when she had become chief of the chemistry laboratory at the Institute of Pathology in Hungary. One of the couple’s most significant discoveries is that of the famous enzyme called elastase. The road to this discovery started with their interest in arteriosclerosis. They developed an interest in understanding blood vessel pathology during arteriosclerosis, primarily when it occurs with aging. In particular, Banga and Baló wanted to know what caused the fibers of the blood vessel walls to degrade. They focused on artery tissues with their elastic properties.

They discovered that fibers in isolated sections of elastic arteries could be dissolved by adding an extract of the pancreas. Under the microscope, Banga and Baló noticed that the pancreas extract made the arteries’ elastic fibers swell up, then break up into pieces, and finally dissolve away. It was a remarkable finding because it predicted that pancreatic tissue was a good source of an elastolytic enzyme, which they would later call elastase. That is, the pancreas was loaded with the elastase enzyme. In short, they had been the first to discover that an elastase enzyme dissolved the elastic fibers of arteries. They have been given due credit for being the first investigators to discover elastase.

Elastase is a member of a large group of enzymes called proteases that degrade proteins. The enzyme works to degrade a fibrous protein called elastin. The elastin protein helps live organisms because it makes fibers that give tissues like skin, lungs, and blood vessels an elastic property. Such tissues need to expand to accommodate their specific functions. Skin needs to stretch, allowing the body to move. Breathing lungs undergo expansion and contraction. Blood vessels have to be elastic to shrink and expand as the heart pumps blood through them.

As Banga and Baló had discovered, the pancreas was a good source of elastase. Because the enzyme destroys elastin, it is made in an inactive form, called a zymogen. The production of a zymogen prevents the inadvertent and unwanted destruction of necessary elastin. The zymogen version of the inactive protease is called proelastase. Another proteolytic enzyme, called trypsin, activates it by cleaving it to make the active elastase. This proteolytic activation by cutting proelastase to make active elastase permits the enzyme to function only during the correct times and places in the body.

Elastic fibers in blood vessels permit expansion and shrinkage to accommodate blood flow. These elastic fibers are made up of individual elastin protein molecules. The fiber networks made of elastin are made inside the cell and secreted to the outside, where they are assembled into so-called extracellular fibers. Starter proteins called tropoelastin are made inside the cells and are transported outside, where they are cross-linked, generating the extracellular fibrous networks.

The elastin molecules are highly hydrophobic proteins and are made up of about 750 amino acids. The elastin molecules are globular or coiled in the relaxed fibrous state, as Banga had predicted, and they are connected in a compacted manner by so-called cross-linkages. When the fibers expand, the elastin molecules uncoil into an extended conformation to permit stretching. When the stretching forces are relieved, the expanded elastins recoil spontaneously to their relaxed fibrous states. Thus, the elastic fibers alternate between relaxed and stretched-out versions. This flexible characteristic of elastin-based fibers brings a certain resiliency to living tissue, a sort of rubbery-like quality.

7) As the years passed, Banga ventured into gerontology—the study of aging—and studied the tissues and the blood vessel walls and the fact that they seem to change over time as we age. Why is this important?

Banga studied aging biochemistry. She focused on protein components of connective tissues, such as elastin and collagen. These molecules undergo extensive cross-linking and amino acid side chain modification with aging. The cross-linking of elastin and collagen in aging tissues gives rise to enhanced rigidity, a property associated with the aging of humans.

In 1954, Banga and Baló did a remarkable experiment. They prepared collagen fibers from rat-tail tendons, added salt solutions, attached them to a tiny amount of lead shot weight, and at room temperature, they watched as the collagen fibers contracted! They had waited about 30 seconds, and the collagen fibers shrank to one-third of their previous length. If they waited about 20 minutes, the contracted fibers would relax back to their original length. Furthermore, Banga and Baló could coax the rat collagen fibers to contract and relax at will. They heated the rat-tail tendon fibers and observed faster rates of contraction and relaxation.

Banga and Baló noted that the contracted collagen fibers were elastic and rubber-like in their forms. They also saw that the fiber’s nitrogen-containing protein appeared to decrease as the collagen relaxed. This nitrogenous protein dissolved away as more of the fiber relaxed, but this protein was inside the collagen fiber. The collagen fibers’ springy elastic character predicted that removing them with elastase would somehow affect the contraction behavior. They knew, however, that their elastase enzyme dissolved the outer nitrogen-containing protein, leaving the internal protein alone. When elastase was put to the test, the collagen fiber contracted! A relaxed fiber was somehow unaffected by elastase. Thus, Banga and Baló concluded that two different proteins were involved in the makeup of collagen fibers.

Today we understand that a typical animal cell has connective tissue with an external matrix encompassing collagen fibers consisting of smaller fibril units made of internal collagen molecules. An internal collagen protein inside the fibril takes the form of a so-called triple helix.

The second protein that Banga had predicted to make up a collagen fiber was likely proteoglycan. These extracellular matrix proteins consist of long chains of sugar linked to a protein core and are typically embedded in the membrane of living cells. The proteoglycan cores are made up of so-called glycosaminoglycan chains, which occupy large amounts of extracellular space and function to regulate cell behaviors.

The biochemical changes that occur in the side-chains of amino acids of collagen and elastin result in dysfunctional interactions between cells and their extracellular matrix materials. These altered cellular and cell-matrix associations can affect the normal functions of the skin, tendons, lungs, and blood vessels. During aging, there are reductions in a person’s ability to replace worn-out collagen, making these tissues lose their necessary functions. Because of age-related changes in the biochemistry of elastin and collagen, the aging body undergoes biological changes. With aging, abnormal elastin molecules accumulate, and the elastin fibers are interrupted. Thus, the skin becomes slightly thinner and less dense, making it looser. Further, the collagen matrix shrinks because the amounts of individual collagen molecules decrease with age. These age-related changes in elastin and collagen lead to the formation of wrinkles in the skin.

We also know that during aging, the levels of elastase enzyme are related. The enzyme seems to increase with advancing age. However, in the late 1970s, researchers from clinical geriatric research laboratories, such as one facility in Tokyo, Japan, followed up on Banga’s insights regarding elastase and arterial aging with developing anti-atherosclerotic therapeutic agents. Surprisingly, they came up with a pancreatic elastase-1 enzyme from porcine as a form of treatment. In their hands, the pig elastase-1 drug improved the clinical condition of atherosclerotic carotid arteries in patients receiving the experimental agent.

The role of elastin and elastase has been somewhat clarified in recent years. During aging, it is believed that tissues harboring elastin are lined with bigger lipid and lipoprotein amounts that increase elastase production levels. The precise reasons for these conflicting data are unknown. Whatever the case, the biochemical and cell biological roles of elastase, elastin, and the cell-matrix material continue to be areas of active investigation. In some so-called “anti-aging” intervention preparations, individual forms of elastin are components. Gerontologists, who typically purport the more reliable healthy roles of proper diet, exercise, and avoidance of smoking, question these sorts of elastin-containing and other such anti-aging topical interventions.

8) How did she spend her final years, and for what is Banga most well known?

Banga has been credited with contributing to several significant lines of scientific research. Banga figured prominently in the discovery of vitamin C. She participated in key laboratory experiments in which vitamin C was isolated from paprika. She was also the first investigator to discover the enzyme elastase and its role in elastin formation and arteriosclerosis. Bang’s elastase discovery is still a relevant topic of research in cell biology and biochemistry. Elastin holds a prominent role in the cellular makeup of the living cell. Banga is widely known for her involvement in the discovery of myosin in muscle contraction.

In recent times, Banga has been given due credit, though in a delayed manner, for her role as a co-discoverer of actin and actomyosin with Albert Szent-Gyorgyi. Banga and her husband also discovered the various biological roles of collagen, a critical extracellular matrix component in animal cells. As you pointed out above, Banga was also tremendously involved in the cellular mechanisms of tissue aging, such as those seen in blood vessels and other vital organs and tissues. Banga’s final scientific years were spent studying the biochemistry of elastin, the elastase enzyme, and other extracellular matrix components, plus connective tissue of cells lining the circulatory system and its biochemistry during aging.

9) Sadly, she never became a Full Professor at any University—but did accomplish quite a lot for a female of her time during World War II and after that—any last thoughts?

There is a controversial story that Banga was taken off the myosin project, the result of which was to delay or prevent a claim in the discovery of actin, a vital muscle contraction protein. Though it is reported that Banga never made such a claim to it, the controversy has been blamed on Albert Szent-Gyorgyi, himself, who in 1970 at a keynote address at the Marine Biological Laboratory in Woods Hole, MA, made a startling admission. Szent-Gyorgyi was reported to have said that he and Banga had discovered actin. They had encountered a viscous, gelatinous material preparing the muscle protein after overnight storage in the refrigerator. According to laboratory lore, Szent-Gyorgyi and Banga had put their muscle prep on ice overnight to attend another seminar that afternoon. When Szent-Gyorgyi and Banga had returned to the lab in the morning, their muscle myosin prep had developed a think viscous material that had not been seen before. They found the material to be loaded with myosin and another myosin-like protein, which they reasoned had been either actin or a complex of actin and myosin, called actomyosin.

During his keynote address that evening, more than 30 years later, a 77-year old Szent-Gyorgyi went on to state that the actin that he and Banga discovered was later isolated in pure form by F. Bruno Straub, whom Szent-Gyorgyi was reported to have felt sorry for because of his war experience. Hence, Szent-Gyorgyi said he entrusted Straub with the necessary actin isolation that Szent-Gyorgyi and Banga discovered initially. The new proclamation by Szent-Gyorgyi that evening in 1970 was controversial because the entire scientific community had since been under the impression that Straub had been the discoverer of actin. Only Straub’s name was on the first paper in 1939 describing the actin isolation, after all. Szent-Gyorgyi later stuck to his recent claim that Banga had been wronged not to have been given credit for her efforts in actin’s discovery, and he wanted to correct the wrong.

File:Pymol image of the substrate binding groove of the alpha subunit of prolyl hydroxylase.png

Figure 6. The substrate-binding groove in the alpha subunit of prolyl hydroxylase.

Incidentally, vitamin C has relevance to another line of Banga’s research. An enzyme called prolyl hydroxylase is involved in the protein chemistry of collagen, Figure 6. The enzyme converts the amino acid proline to hydroxyproline in collagen. Strikingly, the prolyl hydroxylase requires vitamin C! Without this co-factor, the enzyme fails to conduct its protein chemistry in collagen. The result is scurvy, characterized by lesions of the skin and bleeding from the blood vessels.

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