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The specificity of trypsin

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This article is published in Journal of Biological Chemistry.The article was published on 1939-03-01 and is currently open access. It has received 137 citations till now. The article focuses on the topics: Trypsin.

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Journal ArticleDOI

The preparation and properties of two new chromogenic substrates of trypsin.

TL;DR: Preliminary studies indicate that benzoyl dl -arginine p -nitroanilide hydrochloride is also hydrolyzed by papain, and that of l -LPA is in a more alkaline region than normally found for trypsin substrates.
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A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin.

TL;DR: The spectrophotometric procedure proposed by Schwert and Takenaka has been modified and extended to include the application to N-benzoyl-L-tyrosine ethyl ester and α-p-toluenesulphonyl- L-arginine methyl ester, allowing the determination of traces of chymotrypsin in the presence of relatively large amounts of trypsin.
Journal ArticleDOI

A spectrophotometric determination of trypsin and chymotrypsin

TL;DR: A sensitive spectrophotometric assay for trypsin and chymotrypsin using synthetic substrates has been described.
Journal ArticleDOI

Purification and properties of a new enzyme, NG,NG-dimethylarginine dimethylaminohydrolase, from rat kidney.

TL;DR: A new enzyme, NG, NG-dimethylarginine dimethylaminohydrolase, has been purified to homogeneity from rat kidney and shows the maximum activity at pH 6.5 and requires no cofactor.
Journal ArticleDOI

The specific esterase activity of trypsin.

TL;DR: In the course of an investigation of the inhibition of crystalline pancreatic proteolytic enzymes by specific low molecular weight compounds the discovery was made that crystalline trypsin is likewise a powerful catalyst for the hydrolysis of certain amino acid esters.
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