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- W2053118618 abstract "Limited chymotryptic cleavage of the α subunits in the solubilized ATPase from Streptococcus faecalis is accompanied by loss of membrane binding capacity (Abrams, A., Morris, D., Jensen, C. (1976) Biochem. 15, 5560). To obtain evidence that the α chains might function directly in membrane attachment we compared the effect of chymotrypsin on the soluble and membrane-bound enzyme. Using a low level of chymotrypsin the soluble ATPase was quantitatively converted to a catalytically active form in which the 55000 dalton α chains were shortened by approximately 2000 daltons. However, at 80 fold higher levels of chymotrypsin the ATPase in a reconstituted ATPase-membrane complex was completely unaffected. Protection from chymotryptic attack appeared to be membrane specific since the soluble ATPase was not protected by addition of massive amounts of bovine serum albumin. The total and specific immunity to chymotrypsin conferred by membrane binding indicates that chymotrypsin-sensitive α chain “tails” are closely associated with or buried in the membrane. These findings support the view that the α chains are involved directly in membrane attachment." @default.
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- W2053118618 date "1978-03-01" @default.
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- W2053118618 title "Accessibility of the α chains in membrane-bound and solubilized bacterial ATPase to chymotryptic cleavage" @default.
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- W2053118618 doi "https://doi.org/10.1016/0006-291x(78)91553-x" @default.
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