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 Wolfenstein, C. Articles by Listowsky, I. Search for Related Content PubMed PubMed Citation Articles by Wolfenstein, C. Articles by Listowsky, I. Social Bookmarking                      What's this?

Bovine Heart Malic Dehydrogenases

VIII. SUBUNIT STRUCTURE AND MOLECULAR WEIGHT OF THE SUPERNATANT ENZYME

From the ¹ From the Department of Biochemistry, Albert Einstein College of Medicine, Yeshiva University, New York, New York 10461

The molecular weight of bovine heart supernatant malic dehydrogenase has been determined by sedimentation equilibrium. The enzyme was shown to be a dimer with a molecular weight of 72,000. Upon reaction with maleic anhydride or in the presence of guanidinium chloride, the enzyme was dissociated into two subunits having identical molecular weights of about 37,000 as determined by sedimentation equilibrium. These results were confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and peptide mapping experiments. The COOH-terminal amino acid residue of both subunits was identified as alanine, and cleavage by carboxypeptidase digestion did not affect the catalytic activity of the enzyme. Circular dichroism measurements showed that the dissociation of the enzyme by maleic anhydride and guanidinium chloride was accompanied by significant amounts of unfolding in the protein.

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