[Purification of leucine-endopeptidase from Saccharomyces cerevisiae inner mitochondrial membrane].
Several proteolytic activities have been extracted from isolated yeast mitochondrial inner membranes, in the presence of Tween 20. Absence of matrix and cytoplasmic contamination has been checked. A leucine-endopeptidase has been purified to homogeneity. It has an apparent molecular mass of 66 kDa and a pHi near 8.6. It is a serine-protease, which hydrolyses synthetic polypeptides whose leucine carboxylic group is engaged, as well as various macromolecular proteins; its optimal pH is 7.2.
Département d'Immunopharmacologie, Université Louis-Pasteur, Faculté de Pharmacie, Illkirch.
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Pirman
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Stahl
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D066298:In Vitro Techniques; D007425:Intracellular Membranes / Q000201:enzymology*; D007930:Leucine; D008928:Mitochondria / Q000648:ultrastructure*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000648:ultrastructure; D013379:Substrate Specificity
D010450:Endopeptidases; D007930:Leucine
Purification d'une leucine-endopeptidase de la membrane mitochondriale interne de Saccharomyces cerevisiae.