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.
Original language | English (US) |
---|---|
Pages (from-to) | 746-751 |
Number of pages | 6 |
Journal | Journal of Biological Chemistry |
Volume | 262 |
Issue number | 2 |
State | Published - 1987 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology