[Biosynthesis of thiamine triphosphate and identification of thiamine diphosphate-binding proteins in the rat liver hyaloplasm].
The nature of the thiamine diphosphate binding proteins from rat liver hyaloplasm was studied. When [14C]thiamine was used as a marker, a [14C]thiamine diphosphate-containing electrophoretically homogeneous protein preparation was isolated from the liver soluble fraction and classified as transketolase. No other non-enzymatic proteins which bind thiamine diphosphate and can serve as substrates in the reaction of thiamine diphosphate synthesis in the hyaloplasm were found. It was shown that the phosphate group is transferred by rat liver thiamine diphosphate kinase to the free (but not to the protein-bound) thiamine diphosphate as it was believed earlier.
D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism; D002850:Chromatography, Gel; D003593:Cytoplasm / Q000201:enzymology / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008099:Liver / Q000201:enzymology / Q000378:metabolism*; D010770:Phosphotransferases / Q000302:isolation & purification / Q000378:metabolism*; D017856:Phosphotransferases (Phosphate Group Acceptor); D051381:Rats; D013831:Thiamine / Q000031:analogs & derivatives*; D013832:Thiamine Deficiency / Q000201:enzymology / Q000378:metabolism; D013838:Thiamine Triphosphate / Q000096:biosynthesis*; D014174:Transketolase / Q000378:metabolism
D002352:Carrier Proteins; D013838:Thiamine Triphosphate; D014174:Transketolase; D010770:Phosphotransferases; D017856:Phosphotransferases (Phosphate Group Acceptor); C022733:thiamin-diphosphate kinase; D013831:Thiamine
Biosintez tiamintrifosfata i identifikatsiia tiamindifosfatsviazyvaiushchikh belkov gialoplazmy pecheni krys.