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FEBS Lett ; 329(1-2): 47-50, 1993 Aug 23.
Article in English | MEDLINE | ID: mdl-8354406

ABSTRACT

Homogenous ATP-dependent protease has been isolated for the first time from mitochondria of yeast Saccharomyces cerevisiae. The enzyme molecule consists of six 120 kDa subunits. It is a serine protease with an absolute ATP requirement for its activity. Basic enzymatic characteristics of the yeast protease are similar to those of the corresponding rat mitochondrial enzyme and of the E. coli protease La. The yeast enzyme immunochemically cross-reacts with the bacterial protease La.


Subject(s)
Heat-Shock Proteins/isolation & purification , Saccharomyces cerevisiae/enzymology , Serine Endopeptidases/isolation & purification , ATP-Dependent Proteases , Adenosine Triphosphate/pharmacology , Animals , Blotting, Western , Chromatography, High Pressure Liquid , Electrophoresis, Polyacrylamide Gel , Escherichia coli/enzymology , Heat-Shock Proteins/chemistry , Heat-Shock Proteins/metabolism , Magnesium/pharmacology , Mitochondria/enzymology , Molecular Weight , Rats , Serine Endopeptidases/chemistry , Serine Endopeptidases/metabolism
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