Thiamine Pyrophosphatase from Rabbit Brain

John Cooper

doi:10.1016/0076-6879(71)18308-5

Thiamine Pyrophosphatase from Rabbit Brain

John Cooper

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Abstract

This chapter presents the procedure for assay and purification of thiamine pyrophosphatase. Thiamine pyrophosphatase has been purified from liver as well as brain. In both tissues, it appears to have an absolute specificity for thiamine pyrophosphate (TPP) as substrate among the various thiamine phosphate esters, but in addition, it also catalyzes the hydrolysis of certain nucleoside diphosphates. For both the liver and brain enzymes, adenosine triphosphate has an allosteric effect and lowers the K_m of the substrate regardless of whether it is a nucleoside diphosphate or TPP.

Original language	English
Pages (from-to)	227-229
Number of pages	3
Journal	Methods in Enzymology
Volume	18
DOIs	https://doi.org/10.1016/0076-6879(71)18308-5
Publication status	Published - 1 Jan 1970

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AB - This chapter presents the procedure for assay and purification of thiamine pyrophosphatase. Thiamine pyrophosphatase has been purified from liver as well as brain. In both tissues, it appears to have an absolute specificity for thiamine pyrophosphate (TPP) as substrate among the various thiamine phosphate esters, but in addition, it also catalyzes the hydrolysis of certain nucleoside diphosphates. For both the liver and brain enzymes, adenosine triphosphate has an allosteric effect and lowers the Km of the substrate regardless of whether it is a nucleoside diphosphate or TPP.

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ER -

Thiamine Pyrophosphatase from Rabbit Brain

Abstract

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