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- W1586954919 abstract "Chymotryptic digestion of bovine brain uncoating ATPase produced a 60-kDa fragment that was subsequently proteolyzed to 44 kDa. Loss of clathrin cage uncoating activity paralleled the conversion of the intact 70-kDa enzyme to the 60-kDa fragment, while clathrin binding activity was lost as the 60-kDa fragment was degraded to 44 kDa. This 44-kDa fragment has been purified to homogeneity and characterized as a clathrin-independent ATPase. The 44-kDa ATPase domain has been localized within the intact enzyme by the use of amino-terminal specific antibodies. This localization relates to the conserved nature of the 70-kDa heat shock protein family, of which bovine brain uncoating ATPase is a constitutively expressed member." @default.
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- W1586954919 date "1987-01-01" @default.
- W1586954919 modified "2023-09-28" @default.
- W1586954919 title "The ATPase core of a clathrin uncoating protein." @default.
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- W1586954919 doi "https://doi.org/10.1016/s0021-9258(19)75848-7" @default.
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