Background
Moses Kunitz was born on December 19, 1887 in Slonim, Russia (now Belarus).
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Moses Kunitz was born on December 19, 1887 in Slonim, Russia (now Belarus).
Kunitz was educated in Slonim before his immigration to the United States. Kunitz settled in New York City, pursuing his education on a part-time basis at the Cooper Union Evening School of Chemistry, which he entered in 1910.
Kunitz graduated from Cooper Union in 1916 with a Bachelor of Science and then spent two years at Cooper Union's Electrical Engineering School, transferring in 1919 to the Columbia University School of Mines, Engineering, and Chemistry. In 1922, Kunitz became a graduate student at Columbia. He received a Doctor of Philosophy in biological chemistry.
Kunitz settled in New York City in 1909 and obtained work in a hat factory.
In 1913, Kunitz became a laboratory assistant to Jacques Loeb, an eminent cell physiologist, at the Rockefeller Institute in New York City; he remained there for the rest of his scientific career, a period spanning almost sixty years. Loeb, head of the department of physiology at Rockefeller, valued Kunitz's adept and meticulous lab work and encouraged him to pursue a research career.
In 1924 Kunitz was appointed to the staff of the Rockefeller Institute with the title of assistant. Kunitz published his first papers on protein behavior with Loeb in 1923. After Loeb's death in 1924, John Howard Northrop became head of the department of general physiology. Kunitz's collaboration with Northrop in determining the chemical nature of enzymes, which had mystified scientists for a century, constitutes his major contribution to science. Kunitz was made an associate at the Rockefeller Institute in 1926, the year the physiology department moved to Princeton, New Jersey.
Kunitz's knowledge of the chemistry and physical properties of proteins had been gained through his experiments with gelatin under Loeb; Northrop, who had devised a thesis regarding the protein nature of enzymes in the mid-1920's, called upon Kunitz to put that knowledge to the test. Northrop and Kunitz collaborated on the isolation of the two major digestive enzymes, pepsin and trypsin, in crystalline form in 1930 and 1931, and in the decades that followed Kunitz isolated some eighteen additional enzymes and precursors in crystalline form, confirming Northrop's thesis that enzymes are proteins and further elucidating their high specificity in biological reactions.
Responding to a request by the Office of Scientific Research and Development during World War II, Kunitz isolated hexokinase in crystalline form; this enzyme was thought to be involved in the action of mustard gas upon living tissue. Kunitz, who had been made a full member of the Rockefeller Institute in 1949, returned to New York in 1950 when the Princeton branch of the institute was closed. In 1953, with the conversion of the Rockefeller Institute to university status, he became professor emeritus, a title he held until his retirement in 1972. He spent numerous summers working at the Marine Biological Laboratory in Woods Hole, Massachussets, to which he commuted from his summer home in Falmouth Heights, Massachussets.
Kunitz was one of the first researchers to demonstrate that certain inhibiting proteins of the stomach and pancreas prevent digestive enzymes from breaking down the living tissues in which they are formed. One of his papers, "The Kinetics and Thermodynamics of Reversible Denaturation of Crystalline Soybean Trypsin Inhibitor" (1948), demonstrated the process whereby denatured proteins are restored to their original or normal condition. Called by Roger Herriott the "crystallizer of last resort for many younger enzyme chemists, " Kunitz demonstrated a remarkable ability to isolate compounds in the laboratory and pioneered the methodology for enzyme purification. In 1940 he crystallized ribonuclease, the enzyme responsible for the scission of ribonucleic acid (RNA) in living cells; in 1948 he did the same with deoxyribonuclease. This work became particularly important in later biomedical studies of the chemistry of the nucleic acids. Kunitz's work on the purification of proteins opened the door to other medical breakthroughs, including the purification of bacteriophage and the crystallization of diphtheria antitoxin by Northrop, and the crystallization of tobacco mosaic virus by another colleague, Wendell M. Stanley. Kunitz received the Carl Neuberg Medal of the American Society of European Chemists and Pharmacists in 1957. His researches, laid out in papers described as models of scientific reporting, contributed in the short term to scientific breakthroughs that enabled his colleagues Northrop and Stanley to share the Nobel Prize for chemistry in 1946, and in the long term to important advances in enzymology that bioscientists continue to build upon.
Described by his colleagues as a self-effacing man who was uncomfortable in the spotlight, Kunitz "did not write reviews that integrated his studies into the developing thought of the time, " but concentrated his energy and scientific resourcefulness on the task at hand.
Kunitz married Sonia Bloom in 1912. They had two children. After the death of his wife in 1938, he married Rebecca Shamaskin, an émigré from Slonim, in 1939.
