Document Detail

Comparison of the ATPase activities of bovine heart and liver mitochondrial ATP synthases with different tissue-specific gamma subunit isoforms.
MedLine Citation:
PMID:  8179599     Owner:  NLM     Status:  MEDLINE    
The kinetics of heart and liver mitochondrial ATPase (FoF1) were examined using submitochondrial particles (SMPs) purified from the two tissues to obtain information on the role of gamma subunit isoforms. The F1 portion is mainly composed of the catalytic, common alpha beta subunits and tissue-specific gamma subunits. In contrast to the previous reports on the kinetics and crystallography of various F1's, the Vmax and Km of the two isoforms of FoF1 were identical although the SMPs were prepared from different tissues. Moreover sodium azide inhibited the two equally. The ATPase activity of liver SMP showed slightly steeper pH-dependency than that of heart SMP but the pH optima of the two were the same (pH 8).
C Matsuda; E Muneyuki; H Endo; M Yoshida; Y Kagawa
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Publication Detail:
Type:  Comparative Study; In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  200     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1994 Apr 
Date Detail:
Created Date:  1994-06-03     Completed Date:  1994-06-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  671-8     Citation Subset:  IM    
Department of Biochemistry, Jichi Medical School, Tochigi, Japan.
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MeSH Terms
Azides / pharmacology
Hydrogen-Ion Concentration
Mitochondria, Heart / enzymology*
Mitochondria, Liver / enzymology*
Protein Conformation
Proton-Translocating ATPases / antagonists & inhibitors,  chemistry,  metabolism*
Sodium Azide
Submitochondrial Particles / enzymology
Tissue Distribution
Reg. No./Substance:
0/Azides; 26628-22-8/Sodium Azide; EC ATPases

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