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J. Biochem, 1988, Vol. 103, No. 4 678-681
© 1988 Japanese Biochemical Society

research-article

Thiamine Pyrophosphatase (Nucleoside Diphosphatase) in the Golgi Apparatus Is Distinct from Microsomal Nucleoside Diphosphatase

Shin-ichiro Sano, Yoshihiro Matsuda1 and Hachiro Nakagawa

Division of Protein Metabolism, Institute for Protein Research, Osaka University Suita, Osaka 565

1To whom correspondence should be addressed.

The properties of thiamine pyrophosphatase in the Golgi apparatus of rat liver were studied. Thiamine pyrophosphatase in an extract of the Golgi apparatus was separated into 6 bands of between pH 5.4 and 6.3 by isoelectric focusing on polyacrylamide gel. On the gels all these subforms catalyzed the hydrolyses of GDP, IDP, UDP, and CDP as well as that of thiamine pyrophosphate. The characteristics resembled those of Type B nucleoside diphosphatase of rat brain, though the enzyme did not have 3 subforms of Type B nucleoside diphosphatase in the higher pH region on isoelectric focusing. Thiamine pyrophosphatase of the Golgi apparatus was separated from microsomal nucleoside diphosphatase by DEAE-cellulose column chromatography. The properties of the enzyme were quite similar to those of Type B nucleoside diphosphatase with respect to its substrate specificity, optimum pH for activity, and inhibition by ATP. These findings suggest that thiamine pyrophosphatase in the Golgi apparatus is different from microsomal nucleoside diphosphatase and that it might be basically the same enzyme as Type B nucleoside diphosphatase except for different extents of modification.


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