HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Chang, S. H. Articles by With the technical assistance of Norma H. Best, Search for Related Content PubMed PubMed Citation Articles by Chang, S. H. Articles by With the technical assistance of Norma H. Best, Social Bookmarking                      What's this?

Participation of the Unsymmetrical Disulfide of Coenzyme A and Glutathione in an Enzymatic Sulfhydryl-Disulfide Interchange

I. PARTIAL PURIFICATION AND PROPERTIES OF THE BOVINE KIDNEY ENZYME

From the ¹ From the Department of Biochemistry, Agricultural Experiment Station, Oklahoma State University, Stillwater, Oklahoma 74074

An enzyme that catalyzes the following sulfhydryl-disulfide interchange reaction has been purified 180-fold from bovine kidney.

GSH + CoASSG GSSG + CoA-SH

In addition, it has been detected in most rat tissues studied. Its pH optimum is 8.2 and the equilibrium constant for the reaction is near unity at pH 6.9 and 25°. Michaelis constants for reduced glutathione and CoASSG are 3.3 x 10^-4 m and 4.5 x 10^-5 m, respectively. The molecular weight of the enzyme, determined by gel filtration, is approximately 12,000. Several unsymmetrical disulfides containing a glutathione residue are equally as effective as substrates. The enzyme, which becomes less active during storage, is largely reactivated by GSH. Its potential physiological significance is discussed.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?