In:
Collection of Czechoslovak Chemical Communications, Institute of Organic Chemistry & Biochemistry, Vol. 44, No. 9 ( 1979), p. 2854-2860
Abstract:
A simple method for purification of oligomycin-sensitive ATPase from beef heart mitochondria is described. The isolation procedure is based on short term solubilization of mitochondrial membrane in deoxycholate and 1M-KCl followed by sequential precipitation of hydrofobic proteins and isopycnic centrifugation of crude particulate enzyme on sucrose density gradient. The oligomycin-sesitive ATPase preparation has a specific activity 15-20μmol P/min/mg protein and contains 5% of the total mitochondrial protein which can be separated by SDS-polyacrylamide gel electrophoresis into 13 protein components of relative molecular weight from 6 000 - 65 000 daltons, respectively.
Type of Medium:
Online Resource
ISSN:
0010-0765
,
1212-6950
DOI:
10.1135/cccc19792854
Language:
English
Publisher:
Institute of Organic Chemistry & Biochemistry
Publication Date:
1979