Title

Inactivation of Yeast hexokinase B by Triethyltin Bromide and Reactivation by Dithiothreitol and Glucose

Document Type

Article

Publication Date

9-27-1983

Publisher

American Chemical Society

Source Publication

Biochemistry

Source ISSN

0006-2960

Original Item ID

DOI: 10.1021/bi00289a005

Abstract

Binding of triethyltin bromide to yeast hexokinase B results in a rapid change in the reactivity of the sulfhydryl groups of the molecule. The change was characterized by an increased rate as well as extent of reaction of the -SH groups, and it preceded the onset of inhibition of the enzyme. Rapid gel filtration of the enzyme-triethyltin complex reversed this change in sulfhydryl reactivity, and when the eluted enzyme was subjected to short incubation periods, the slow inhibition that occurs with the unfiltered enzyme-triethytin complex was no longer manifested. With prolonged incubation, however, the gel-filtered sample demonstrated increased rate of loss of enzyme activity, indicating that the gel filtration step did not

Comments

Biochemistry, Vol. 22, No. 20 (September 27, 1983): 4642-4646. DOI.

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