CHARACTERIZATION OF HIGH-MOLECULAR-MASS HEAT-SHOCK PROTEINS AND 42-DEGREES-C-SPECIFIC HEAT-SHOCK PROTEINS OF MURINE CELLS

被引:28
作者
HATAYAMA, T
YASUDA, K
NISHIYAMA, E
机构
[1] Department of Biochemistry, Kyoto Pharmaceutical University, Kyoto, 607, Yamashima Ku
关键词
D O I
10.1006/bbrc.1994.2467
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
There are two isoforms of high-molecular-mass heat shock protein (HMM-HSP), hsp105A and hsp105B, in murine FM3A cells. To characterize the HMM-HSPs, we here purified hsp105A and hsp105B, as well as 42 degrees C-specific HSPs that are specifically induced by continuous heating at 42 degrees C, from the cytoplasmic extracts of the FM3A cells heat shocked at 42 degrees C for 8 h. Digestion of the hsp105A, hsp105B, and 42 degrees C-specific HSPs with lysyl endopeptidase generated 17,000-Da polypeptide fragments in common, and the N-terminal amino acid sequences of the fragments revealed a homology with those of the adenosine binding domain of hsp70 family proteins and actin. Thus, the two isoforms of hspl05 and the 42 degrees C-specific HSPs seemed to be very similar proteins having a ATP binding domain in common, and these HSPs may constitute a HMM-HSP family in murine cells. (C) 1994 Academic Press, Inc.
引用
收藏
页码:357 / 365
页数:9
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