John Howard Northrop

John Howard Northrop passed away on May 27, 1987, in Wickenburg, Arizona. He left behind a legacy as one of the pivotal figures in the study of enzymes and proteins. Throughout his lifetime, Northrop's research contributed significantly to our understanding of enzyme chemistry and biology, and his pioneering work continues to be a cornerstone in biochemical studies.

John Howard Northrop retired from active research on May 8, 1961. His career, marked by significant scientific achievements, especially in the field of biochemistry and enzymology, spanned several decades. Even after retiring, Northrop's work continued to influence the scientific community, as his methodologies and findings provided a foundation for future biochemical research.

In 1950, Northrop published a comprehensive and definitive work on the biological and chemical properties of enzymes. This publication compiled years of research and became an essential reference for scientists studying enzymology. Northrop's extensive work in enzyme purification and characterization helped solidify understandings of enzyme kinetics and mechanisms.

In 1949, John Howard Northrop became a Professor of Bacteriology and a member of the Department of Bacteriology at the University of California, Berkeley. At Berkeley, he continued his research on enzymes, sharing his expertise with both students and colleagues. This position allowed him to influence the next generation of scientists through his innovative work and teaching.

On December 10, 1946, John Howard Northrop was jointly awarded the Nobel Prize in Chemistry along with James Batcheller Sumner and Wendell Meredith Stanley. The Nobel Prize recognized his significant contributions to the preparation of enzymes and virus proteins in a pure form. Northrop's work facilitated the detailed study of enzyme activity and structure, revolutionizing the field of biochemistry.

In 1939, John Howard Northrop published the influential book 'Crystalline Enzymes,' detailing his research and techniques related to enzyme crystallization. The book provided significant insights into protein chemistry and the methodologies for obtaining crystalline forms of enzymes. This publication cemented Northrop's position as a leading figure in the study of macromolecular biology and enzymology.

In the year 1930, John Howard Northrop successfully isolated the enzyme pepsin, a digestive protease found in the stomach. This achievement was crucial in obtaining pure and stable forms of enzymes, which furthered biochemical research by allowing for the study of enzyme structures and functions. Pepsin was one of the first enzymes to be crystallized, showcasing Northrop's expertise in the purification and crystallization of proteins.

In 1915, John Howard Northrop was awarded a Ph.D. in chemistry from Columbia University. His doctoral studies and research focused on the field of chemistry, leading to a distinguished career dedicated to biochemistry. His education laid the foundation for groundbreaking work in enzyme isolation and protein crystallization.

John Howard Northrop was born on July 5, 1891, in Yonkers, New York. He was the son of John I. Northrop, a professor of zoology, and Alice Rich Northrop, a teacher and botanist. His upbringing in a scientifically oriented family set the stage for his illustrious career in biochemistry and the study of enzymes.