Document Detail

Proteolytic interconversion of electrophoretic variants of the enzyme rhodanese.
MedLine Citation:
PMID:  6571838     Owner:  NLM     Status:  MEDLINE    
It has been confirmed that the enzyme rhodanese, although a homogeneous single polypeptide chain protein by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, is separable by electrophoresis under nondenaturing conditions into four species which differ in net surface charge (I-IV in the order of increasing positive charge). Limited proteolysis can interconvert these species. Chymotrypsin converts IV and III to II and forms a small amount of I. Carboxypeptidase B converts IV to III. The total protein among the species remains constant, and two-dimensional gels show that the change induced is below the resolution of the sodium dodecyl sulfate-polyacrylamide gel system. The suggestion that the products can be produced in the order IV, III, and II is supported by the results of sequential treatment of rhodanese first with carboxypeptidase B and then with chymotrypsin. It is concluded that there are covalent differences among the rhodanese species identified to date and an interconversion of forms can be triggered by proteolysis at the COOH-terminal end of the Mr = 33,000 single polypeptide chain which comprises the enzyme. This conclusion is strengthened by the close similarity between the amino acid composition of the peptide released by chymotrypsin and the composition expected on the basis of the known sequence. Furthermore, it appears that form IV is the primary in vivo product and the other species arise from it.
P Horowitz; K Falksen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  258     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1983 Feb 
Date Detail:
Created Date:  1983-03-17     Completed Date:  1983-03-17     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1614-8     Citation Subset:  IM    
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MeSH Terms
Carboxypeptidase B
Electrophoresis, Polyacrylamide Gel
Genetic Variation*
Peptide Fragments / metabolism
Sulfurtransferases / metabolism*
Thiosulfate Sulfurtransferase / genetics,  metabolism*
Grant Support
Reg. No./Substance:
0/Peptide Fragments; EC 2.8.1.-/Sulfurtransferases; EC Sulfurtransferase; EC 3.4.-/Carboxypeptidases; EC B; EC

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