[Isolation and various properties of thiamine-binding protein from synaptosomes in the rat brain].
A thiamine-binding protein (ThBP) with a specific activity of 8.21 nmoles/mg protein was isolated from rat brain synaptosomes by affinity chromatography and gel filtration on Sephadex G-200. The protein was purified 746-fold with a 40.5% yield. ThBP was homogeneous during sodium dodecyl sulfate gel electrophoresis; its molecular mass was determined by gel filtration on Sephadex G-200 and by sodium dodecyl sulfate gel electrophoresis and was equal to 107 and 103 kD, respectively. The pH optimum for the binding is 8.35. When the ability of ThBP to bind thiamine phosphates was tested, the latter decreased in the following order: thiamine monophosphate greater than thiamine triphosphate greater than greater than thiamine diphosphate.
Postoenko
V A
VA
Parkhomenko
Iu M
IuM
Vovk
A I
AI
Khalmuradov
A G
AG
Donchenko
G V
GV
D000818:Animals; D001923:Brain Chemistry; D002352:Carrier Proteins / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008297:Male; D008970:Molecular Weight; D051381:Rats; D013574:Synaptosomes / Q000032:analysis*; D013831:Thiamine / Q000302:isolation & purification*
D002352:Carrier Proteins; C026989:thiamine-binding protein; D013831:Thiamine
Vydelenie i nekotorye svoĭstva tiaminsviazyvaiushchego belka sinaptosom golovnogo mozga krys.