Document Detail

Inactivation of phosphorylase b by potassium ferrate. Identification of a tyrosine residue involved in the binding of adenosine 5'-monophosphate.
MedLine Citation:
PMID:  670209     Owner:  NLM     Status:  MEDLINE    
The site of reaction of potassium ferrate (K2FeO4) with rabbit muscle phosphorylase b has been further characterized in an extension of previously published studies (Lee, Y. M., and Benisek, W. F. (1976) J. Biol, Chem. 251, 1553-1560) reporting inactivation of the enzyme by this reagent. The tryptic peptide composed of residues 70 to 80 of the enzyme's polypeptide chain was shown to contain a tyrosine residue which is chemically modified by ferrate and which is protected by 5'-AMP. The sequence of this peptide obtained from both untreated and ferrate-treated phosphorylase b was determined, and the results showed that tyrosine-75 was the residue with which ferrate reacts.
Y M Lee; W F Benisek
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  253     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1978 Aug 
Date Detail:
Created Date:  1978-09-15     Completed Date:  1978-09-15     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5460-3     Citation Subset:  IM    
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MeSH Terms
Adenosine Monophosphate*
Amino Acid Sequence
Binding Sites
Iron* / pharmacology
Muscles / enzymology
Peptide Fragments / analysis
Phosphorylases* / antagonists & inhibitors
Protein Binding
Reg. No./Substance:
0/Peptide Fragments; 55520-40-6/Tyrosine; 61-19-8/Adenosine Monophosphate; 7439-89-6/Iron; EC 2.4.1.-/Phosphorylases

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