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A colorimetric method for the determination of chymotrypsin activity

Iselin, Beat M. and Huang, H. T. and Niemann, Carl (1950) A colorimetric method for the determination of chymotrypsin activity. Journal of Biological Chemistry, 183 (2). pp. 403-407. ISSN 0021-9258. http://resolver.caltech.edu/CaltechAUTHORS:ISEjbc50b

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Abstract

The L isomers of esters, amides, and hydrazides of the general formula RCONHCHR1COR2 where R = CH3-, C6H5-, etc., R1 = C6H6CH2-, p-HO-C6H4CH2-, etc., and R2 = -OCH3, -NH2, or -NHNH2, are known to be hydrolyzed by chymotrypsin (l-6). It has now been found that the corresponding hydroxamides, RCONHCHR1CONHOH, where R1 = C6H5CH2-, are also hydrolyzed by this enzyme (Table I). Aside from the obvious usefulness of the above hydroxamides in the further definition of chymotrypsin activity we wish to point out that these latter substrates provide the basis for a simple, sensitive, and rapid calorimetric method for the determination of chymotrypsin activity which can be extended to a number of other proteolytic enzymes.


Item Type:Article
Additional Information:Copyright © 1950 by the American Society of Biological Chemists (Received for publication, October 31, 1949) Supported in part by a grant from Eli Lilly and Company. Contribution No. 1348 from the Gates and Crellin Laboratories of Chemistry, California Institution of Technology, Pasadena
Record Number:CaltechAUTHORS:ISEjbc50b
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:ISEjbc50b
Alternative URL:http://www.jbc.org/content/vol183/issue2/index.shtml
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:4599
Collection:CaltechAUTHORS
Deposited By: Archive Administrator
Deposited On:29 Aug 2006
Last Modified:26 Dec 2012 09:00

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