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GTP modulates calcium binding and cation-induced conformational changes in erythrocyte transglutaminase.

Authors
  • Bergamini, C M
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Nov 07, 1988
Volume
239
Issue
2
Pages
255–258
Identifiers
PMID: 2903073
Source
Medline
License
Unknown

Abstract

Calcium binding to erythrocyte transglutaminase was determined by equilibrium dialysis. Results indicate that 6 ions are bound to the enzyme both in the absence and in the presence of GTP and that the nucleotide reduces the affinity of the enzyme for calcium. Furthermore, I- fluorescence quenching and proteolytic inactivation experiments proved that GTP also alters the conformation of the enzyme. It is thus suggested that multiple mechanisms are involved in the regulation of the enzyme activity by GTP.

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