Thiamine triphosphatase in the nervous system

Robert L. Barchi; Peter E. Braun

doi:10.1016/0005-2736(72)90040-5

Thiamine triphosphatase in the nervous system

Robert L. Barchi, Peter E. Braun

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Thiamine triphosphate is hydrolyzed by a specific triphosphatase in subcellular fractions of rat brain. This enzyme differs from nucleoside triphosphatases in (1) its subcellular distribution pattern; (2) its susceptibility to inhibition by Ca²⁺; (3) its activation by sodium deoxycholate; (4) its failure to be affected by known inhibitors of other triphosphatases. The specific activity of the thiamine triphosphatase is as high as that of Mg²⁺-activated ATPase.

Original language	English (US)
Pages (from-to)	402-405
Number of pages	4
Journal	BBA - Biomembranes
Volume	255
Issue number	1
DOIs	https://doi.org/10.1016/0005-2736(72)90040-5
State	Published - Jan 17 1972
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Cell Biology

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AB - Thiamine triphosphate is hydrolyzed by a specific triphosphatase in subcellular fractions of rat brain. This enzyme differs from nucleoside triphosphatases in (1) its subcellular distribution pattern; (2) its susceptibility to inhibition by Ca2+; (3) its activation by sodium deoxycholate; (4) its failure to be affected by known inhibitors of other triphosphatases. The specific activity of the thiamine triphosphatase is as high as that of Mg2+-activated ATPase.

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Thiamine triphosphatase in the nervous system

Abstract

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