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James B. Sumner

James B. Sumner is a chemistry topic covered in the lgStudy science library. This page brings together a partial reference excerpt, illustrations, worked examples, real-world applications and a short study plan, so you can understand James B. Sumner rather than just read about it. In short: James Batcheller Sumner (November 19, 1887 – August 12, 1955) was an American biochemist. He discovered that enzymes can be crystallized, for which he shared the Nobel Prize in Chemistry in 1946 with John Howard Northrop and Wendell Meredith Stanley.

James B. Sumner — main illustration
James B. Sumner — illustration

Key takeaways

  • James B. Sumner belongs to chemistry; place it in that map before memorising details.
  • Learn the definition first, then one example that makes the definition concrete.
  • Connect James B. Sumner to a quantity you can measure, compute or draw — that is where exam questions come from.
  • Reproduce the core statement of James B. Sumner from memory before moving on to harder problems.

Reference excerpt

James Batcheller Sumner (November 19, 1887 – August 12, 1955) was an American biochemist. He discovered that enzymes can be crystallized, for which he shared the Nobel Prize in Chemistry in 1946 with John Howard Northrop and Wendell Meredith Stanley. He was also the first to prove that enzymes are proteins.

Biography Sumner was born on November 19, 1887, in Canton, Massachusetts. While hunting at age 17, Sumner was accidentally shot by a companion and as a result his left arm had to be amputated just below the elbow. He had been left-handed before the accident, after which he had to learn to do things with his right hand. Sumner graduated from Harvard University with a bachelor's degree in 1910 where he was acquainted with prominent chemists Roger Adams, Farrington Daniels, Frank C. Whitmore, James Bryant Conant and Charles Loring Jackson. After a short period of working in the cotton knitting factory owned by his uncle, he accepted a teaching position at Mount Allison University in Sackville, New Brunswick, Canada. For the year 1911-12 he worked as a teaching assistantship in chemistry at Worcester Polytechnic Institute. In 1912, he went to study biochemistry in Harvard Medical School and obtained his Ph.D. degree in 1914 with Otto Folin. He then worked as assistant professor of biochemistry at Cornell Medical School in Ithaca, NY. Sumner married Cid Ricketts (born Bertha Louise Ricketts in Brookhaven, Mississippi) when she attended medical school at Cornell. They married on July 10, 1915, and had four children. They were divorced in 1930, but she kept her married name. Cid Ricketts Sumner went on to become an author, writing books that included Tammy Tell Me True, which was made into the movie Tammy and the Bachelor, and Quality, which became the movie Pinky. Cid Ricketts Sumner was murdered by their grandson, John R. Cutler, in 1970. In 1931 Sumner married Agnes Lundkvist. In 1943 they divorced; later that year he married Mary Beyer, with whom he had two children.

Research It was in 1917 at Cornell where Sumner began his research into isolating enzymes in pure form; a feat which had never been achieved before. The enzyme he worked with was urease, which he isolated from jack beans. Sumner's work was unsuccessful for many years and many of his colleagues were doubtful, believing that what he was trying to achieve was impossible, but in 1926 he demonstrated that urease could be isolated and crystallized. He accomplished this by mixing purified urease with acetone and then chilling it; the chilled solution produced crystallized urease. He was also able to show by chemical tests that his pure urease was a protein. This was the first experimental proof that an enzyme is a protein, a controversial question at the time. His successful research brought him to full professorship at Cornell in 1929. From 1924 on his laboratory was located on the second floor of the new dairy science building, Stocking Hall (today home to Food Science), at Cornell where he did his Nobel Prize–winning research. In 1937 he succeeded in isolating and crystallizing a second enzyme, catalase. By this time, John Howard Northrop of the Rockefeller Institute had obtained other crystalline enzymes by similar methods, starting with pepsin in 1929. It had become clear that Sumner had devised a general crystallization method for enzymes, and also that all enzymes are proteins.

Honors and awards In 1937, he was given a Guggenheim Fellowship and he spent five months in Sweden working with Professor Theodor Svedberg. Also that year, he was awarded the Scheele Award in Stockholm. Both Sumner and Northrop, along with Wendell M Stanley, shared the Nobel Prize in 1946 for crystallization of enzymes. In 1947 Sumner became the director of Cornell's enzyme chemistry laboratory. Sumner was elected to the National Academy of Sciences in 1948. In 1949, he was elected a Fellow of the American Academy of Arts and Sciences.

Death Sumner died at age 67 of cancer in Buffalo, New York on August 12, 1955.

References

Further reading James B. Sumner on Nobelprize.org including the Nobel Lecture, December 12, 1946 The Chemical Nature of Enzymes Alexander L. Dounce (1955). "Prof. James B. Sumner". Nature. 176 (4488): 859. Bibcode:1955Natur.176..859D. doi:10.1038/176859a0. "Sumner, James B. (1887–1955)". Biographical Memoirs of the National Academy of Sciences. 31.

External links Sumner's Nobel Lecture The Chemical Nature of Enzymes Sumner's Speech at the Nobel banquet

Illustrations

James B. Sumner illustration

Worked examples

Example 1 — a first encounter with James B. Sumner

Start with the simplest possible case. Write down what James B. Sumner claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In chemistry, the smallest case is usually a single object, a single equation or a single measurement. Check that every symbol or term in your sentence has a meaning in that case.

Example 2 — changing one variable

Take the situation from Example 1 and change exactly one quantity: double it, halve it, or set it to zero. Predict what should happen to James B. Sumner before you calculate. Comparing your prediction with the result is the fastest way to find out whether you understand the idea or only the words.

Example 3 — an exam-style question

Typical questions about James B. Sumner ask you to (a) state it precisely, (b) apply it to given data, and (c) explain a limitation. Practise writing all three answers in under five minutes; the third part is what separates a full-mark answer from an average one.

Applications of James B. Sumner

In research
James B. Sumner appears in chemistry research whenever the underlying quantities have to be modelled precisely. Papers usually cite it as a starting assumption and then explore where it breaks down.
In technology and industry
Engineering practice reuses James B. Sumner in design rules, simulations and safety margins. Knowing the idea lets you read a specification sheet and understand why the numbers look the way they do.
In the classroom
James B. Sumner is common in secondary-school and first-year university syllabi. It links to neighbouring topics 1887 births, 1955 deaths, 20th-century American biochemists, so understanding it makes those chapters shorter.
In everyday life
Look for James B. Sumner outside the textbook — in sport, cooking, traffic, electronics or the sky above you. An example you found yourself is remembered far longer than one you were given.
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How to study James B. Sumner in 20 minutes

  1. Read the reference excerpt below once, without taking notes.
  2. Close the page and write down what James B. Sumner means in your own words.
  3. Compare your version with the excerpt and mark what you missed.
  4. Work through the three examples above with pen and paper.
  5. Explain James B. Sumner out loud to somebody else — or to Teacher Smith in the lgStudy chat.

Frequently asked questions

What is James B. Sumner in simple terms?

James Batcheller Sumner (November 19, 1887 – August 12, 1955) was an American biochemist. He discovered that enzymes can be crystallized, for which he shared the Nobel Prize in Chemistry in 1946 with John Howard Northrop and Wendell Meredith Stanley.

Why does James B. Sumner matter?

Because it connects several chemistry ideas at once: it gives you a definition you can apply, a quantity you can calculate, and a way to check whether a result is plausible.

How should I study James B. Sumner?

Read the excerpt, restate it from memory, then work through the examples and applications listed on this page. The five-step study plan above takes about twenty minutes.

What does this page cover?

It gives you a compact reference excerpt plus original lgStudy explanations, examples, applications and study material on James B. Sumner.

Tags

  • 1887 births
  • 1955 deaths
  • 20th-century American biochemists
  • American Nobel laureates
  • American amputees
  • Cornell University faculty
  • Fellows of the American Academy of Arts and Sciences
  • Harvard Medical School alumni
  • Members of the United States National Academy of Sciences
  • Nobel laureates in Chemistry
  • People from Canton, Massachusetts

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