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 Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Kanji, M. I. Articles by Carper, W. R. Search for Related Content PubMed PubMed Citation Articles by Kanji, M. I. Articles by Carper, W. R. Social Bookmarking                      What's this?

JBC, Vol. 251, Issue 8, 2255-2257, Apr, 1976

Glucose-6-phosphate dehydrogenase. Purification and partial characterization

M. I. Kanji, M. L. Toews and W. R. Carper

Glucose-6-phosphate dehydrogenase has been purified 1000-fold from pig liver. This enzyme exists as an active dimer of molecular weight 133,000 and an inactive monomer of molecular weight 67,500. The pH of maximum activity is 8.5 and the ionic strength maximum is 0.1 to 0.5 M. Glucose-6-phosphate dehydrogenase is highly specific for NADP+ and glucose 6-phosphate. Apparent Km values of 3.6 muM and 5.4 muM were obtained for glucose 6-phosphate and NADP+. This enzyme is located almost entirely within the soluble portion of the cellular cytoplasm.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?