| Literature DB >> 4274131 |
Abstract
A low-molecular-weight protein synthesized in yeast mitochondria was purified. The protein was identified as a component of the rutamycin-sensitive ATPase. The amino-acid composition of the purified protein shows an extremely large preponderance of nonpolar residues, which may account for its solubility in chloroform-methanol. Indirect evidence suggests that this component is involved in the conferral of rutamycin sensitivity and may also have a function in the assembly of the ATPase complex.Entities:
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Year: 1973 PMID: 4274131 PMCID: PMC427191 DOI: 10.1073/pnas.70.11.3155
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205