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 Sibilli, L. Articles by Cohen, G. N. Search for Related Content PubMed PubMed Citation Articles by Sibilli, L. Articles by Cohen, G. N. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 256, Issue 20, 10228-10230, 10, 1981

Two regions of the bifunctional protein aspartokinase I- homoserine dehydrogenase I are connected by a short hinge

L Sibilli, G Le Bras, G Le Bras and GN Cohen

Four proteases differing in their specificity, i.e. subtilisin, trypsin, alpha-chymotrypsin and V8 staphylococcal protease, cleave the bifunctional protein Escherichia coli aspartokinase I-homoserine dehydrogenase I (composed of 820 residues) producing an active homoserine dehydrogenase fragment. This cleavage occurs within a short segment of the polypeptide chain extending from residue 293 to residue 300.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?