PURIFICATION OF A LEUCINE-ENDOPEPTIDASE FROM SACCHAROMYCES-CEREVISIAE INNER MITOCHONDRIAL-MEMBRANE

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作者：
PIRMAN, A
STAHL, A
机构：
来源：
COMPTES RENDUS DE L ACADEMIE DES SCIENCES SERIE III-SCIENCES DE LA VIE-LIFE SCIENCES | 1993年 / 316卷 / 01期
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中图分类号：
Q [生物科学];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
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.
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页码：13 / 19
页数：7
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