[Aggregation of tryptophanyl-tRNA synthetase depending on temperature. Study by a low-angle scatter x-ray method].
By means of small angle X-ray scattering, an aggregation of beef pancreas Trp-tRNA synthetase (EC 6.1.1.2) was observed at physiological temperatures. A Trp-tRNA synthetase preparation which is homogeneous after PAGE in beta-ME-SDS was found to be heterogeneous in particle sizes even at low (4-8 degrees C) temperature. At heating up to 30-45 degrees C, the oligomer sizes increased as well as its proportion depending on the incubation time and temperature; very large aggregates were observed 10 times exceeding the sizes of initial particles. Cooling to 20 degrees C caused no disaggregation due to disulphide bond formation between associated subunits of Trp-tRNA synthetase. A hypothesis is proposed that the aggregation of bovine Trp-tRNA synthetase evaluated in vitro and not observed earlier with any aminoacyl-tRNA synthetases of unicellular organisms might serve as one of the mechanisms of its compartmentation in pancreas.
Tuzikov
F V
FV
Tuzikova
N A
NA
Vavilin
V I
VI
Zinov'ev
V V
VV
Malygin
E G
EG
Favorova
O O
OO
Zargarova
T A
TA
Sudomoina
M A
MA
Kiselev
L L
LL
D000818:Animals; D002417:Cattle; D004220:Disulfides / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D013696:Temperature; D014369:Tryptophan-tRNA Ligase / Q000737:chemistry*; D014961:X-Ray Diffraction
D004220:Disulfides; D014369:Tryptophan-tRNA Ligase
Zavisiashchaia ot temperatury agregatsiia triptofanil-tRNK-sintetazy. Issledovanie metodom malouglovogo rentgenovskogo rasseianiia.