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内蒙古自治区呼和浩特市赛罕区大学西街235号 邮编: 010021
作者机构:JICHI MED SCH DEPT BIOCHEM MINAMIKAWACHI TOCHIGI 32904 JAPAN CHUO UNIV FAC SCI & ENGN DEPT IND CHEM BUNKYO KU TOKYO JAPAN
出 版 物:《BIOCHIMICA ET BIOPHYSICA ACTA》 (Biochim. Biophys. Acta Bioenerg.)
年 卷 期:1988年第933卷第1期
页 面:141-155页
核心收录:
学科分类:0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学]
基 金:Ministry of Education Culture Sports Science and Technology MEXT
主 题:ATP synthase Amino acid sequence Nucleotide sequence Subunit purification Gene expression F 0 F 1 ATP synthase stability F 0 F 1 ATP synthase TF 0 F 1 thermophilic F 0 F 1 F 1 catalytic portion of F 0 F 1 TF 1 thermophilic F 1 EF 1 Escherichi coli F 1 , F 0 , proton channel portion of F 0 F 1 TF 0 thermophilic F 0 EF 0 Escherichia coli F 0 SDS sodium dode-cylsulfate
摘 要:The primary structures of all the subunits of thermophilic ATP synthase were determined, and its .alpha., .beta. and .gamma. subunits could be over-expressed in Escherichia coli, because these subunits were stable and reconstitutable. DNA of 7500 base pairs in length was found to contain a cluster of nine genes for subunits of ATP synthase. The order of their reading frames (size in base pairs) was: I(381):a(630):c(216):b(489):.delta.(537):.alpha.(1507):.gamma.(858):.beta.(1419):.epsilon.(396), I being a gene for a small hydrophobic, basic protein expressed in vitro. All the termini of TF0F1 subunits were confirmed by peptide sequencing. Large quantities of the overexpressed thermophilic .alpha., .beta. and .gamma. subunits were prepared from the extract of E. coli, by a few purification steps.