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ERIC Number: EJ895548
Record Type: Journal
Publication Date: 2010
Pages: 4
Abstractor: As Provided
Reference Count: 5
ISSN: ISSN-1470-8175
Measurement of k[subscript on] without a Rapid-Mixing Device
Kahn, James; Dutnall, Robert N.; Matulef, Kimberly; Plesniak, Leigh A.
Biochemistry and Molecular Biology Education, v38 n4 p238-241 Jul-Aug 2010
We have recently designed a biochemistry laboratory experiment for the purpose of providing students an advanced experience with enzyme kinetics and the kinetics of binding. Bestatin, a well-known and commercially available general protease inhibitor, is a slow-binding inhibitor of aminopeptidase isolated from "Aeromonas proteolytica." The binding is on a timescale slow enough for measurement without the use of a rapid-mixing device. Aminopeptidase inhibition is detected via a standard colorimetric assay with an inexpensive commercially available substrate. The binding of bestatin follows first order binding kinetics with a rate constant k[subscript on] of 59 plus or minus 5 M[superscript -1] s[superscript -1]. This aminopeptidase is well characterized with several crystal structures and a published K[subscript i], which students can then use to calculate the value for k[subscript off]. (Contains 5 figures.)
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Publication Type: Journal Articles; Reports - Descriptive
Education Level: N/A
Audience: Teachers
Language: English
Sponsor: N/A
Authoring Institution: N/A