Measurement of k[subscript on] without a Rapid-Mixing Device

Autor/inn/en	Kahn, James; Dutnall, Robert N.; Matulef, Kimberly; Plesniak, Leigh A.
Titel	Measurement of k[subscript on] without a Rapid-Mixing Device
Quelle	In: Biochemistry and Molecular Biology Education, 38 (2010) 4, S.238-241 (4 Seiten)Infoseite zur Zeitschrift PDF als Volltext Verfügbarkeit
Sprache	englisch
Dokumenttyp	gedruckt; online; Zeitschriftenaufsatz
ISSN	1470-8175
DOI	10.1002/bmb.20369
Schlagwörter	Biochemistry; Laboratory Experiments; Kinetics; Measurement; Science Instruction + Suchen Sie Ihr Suchwort? Biochemie; Laboratory work; Laborarbeit; Kinetik; Messverfahren; Teaching of science; Science education; Natural sciences Lessons; Naturwissenschaftlicher Unterricht
Abstract	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.) (As Provided).
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Erfasst von	ERIC (Education Resources Information Center), Washington, DC
Update	2017/4/10