skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Biosynthesis of thiamine triphosphate and identification of thiamine diphosphate-binding proteins of rat liver hyaloplasm

Journal Article · · Biochemistry (Engl. Transl.); (United States)
OSTI ID:5767682

The nature of the proteins of rat liver hyaloplasm that bind ThDP* was studied. When injection of (/sup 14/C)thiamine was used as the marker, an electrophoretically homogeneous protein preparations, containing (/sup 14/C)ThDP, identified as transketolase, was isolated from the soluble fraction of the liver. No other nonenzymatic proteins that bind ThDP and might serve as the substrate in the synthesis of ThTP were detected in the hyaloplasm. It was shown that transfer of the phosphate group by rat liver ThDP kinase occurs to the free ThDP, and not to protein-bound ThDP, as was previously asserted.

OSTI ID:
5767682
Journal Information:
Biochemistry (Engl. Transl.); (United States), Vol. 50:9; Other Information: Translated from Biokhimiya; 50: No. 9, 1421-1427(Sep 1985)
Country of Publication:
United States
Language:
English

Similar Records

Coenzyme metabolism in rat liver transketolase
Journal Article · Sat Jan 10 00:00:00 EST 1987 · Biochemistry (Engl. Transl.); (United States) · OSTI ID:5767682

Binding of decomposition products of UDP-galactose to the microsomes and polyribosomes isolated from rat liver
Journal Article · Thu Oct 01 00:00:00 EDT 1987 · Biochem. Med. Metab. Biol.; (United States) · OSTI ID:5767682

Identification of high-affinity calmodulin-binding proteins in rat liver
Journal Article · Sun Mar 01 00:00:00 EST 1987 · Am. J. Physiol.; (United States) · OSTI ID:5767682