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Apparently irreversible GTP hydrolysis attends tubulin self-assembly.

作者信息

Angelastro J M, Purich D L

机构信息

Department of Biochemistry and Molecular Biology, University of Florida.

出版信息

Eur J Biochem. 1990 Jul 31;191(2):507-11. doi: 10.1111/j.1432-1033.1990.tb19150.x.

DOI:10.1111/j.1432-1033.1990.tb19150.x
PMID:2384097
Abstract

The pathway of GTP hydrolysis associated with microtubule polymerization was investigated using an assay of intermediate 18O-exchange reactions. Under a variety of conditions influencing tubulin self-assembly, GTP was hydrolyzed without any evidence of multiple reversals characteristic of reversible phosphoanhydride-bond cleavage. These results also accord with published findings that ATP hydrolysis during actin polymerization fails to display intermediate exchange reactions [Carlier, M. F., Pantaloni, D., Evans, J. A., Lambooy, P. K., Korn, E. D. and Webb, M. R. (1988) FEBS Lett. 235, 211-214].

摘要

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