FOLDING INVITRO OF BOVINE PANCREATIC TRYPSIN-INHIBITOR IN THE PRESENCE OF PROTEINS OF THE ENDOPLASMIC-RETICULUM

被引:62
作者
ZAPUN, A
CREIGHTON, TE
ROWLING, PJE
FREEDMAN, RB
机构
[1] EUROPEAN MOLEC BIOL LAB, MEYERHOFSTR 1, W-6900 HEIDELBERG, GERMANY
[2] UNIV KENT, BIOL LAB, CANTERBURY CT2 7NJ, ENGLAND
[3] MRC, MOLEC BIOL LAB, CAMBRIDGE CB2 2QH, ENGLAND
关键词
PROTEIN DISULFIDE ISOMERASE; DISULFIDE BONDS; PROTEIN FOLDING; CHAPERONES;
D O I
10.1002/prot.340140104
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The rates of folding and disulfide bond formation in reduced BPTI were measured in vitro in the presence and absence of total protein from the endoplasmic reticulum. The rates were increased substantially by the endoplasmic reticulum proteins, but only to the extent expected from the known content and activity of protein-disulfide-isomerase. No effects of added ATP or Ca2+ were observed, even though protein-disulfide-isomerase binds Ca2+ tightly.
引用
收藏
页码:10 / 15
页数:6
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