Purification and characterization of small heat shock proteins

被引：30

作者：

Buchner, J ^{[1
]}

Ehrnsperger, M

Gaestel, M

Walke, S

机构：

[1] Univ Regensburg, Inst Biophys & Phys Biochem, D-93040 Regensburg, Germany

[2] Max Delbruck Ctr Mol Med, D-13122 Berlin, Germany

[3] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

来源：

MOLECULAR CHAPERONES | 1998年 / 290卷

关键词：

D O I：

10.1016/S0076-6879(98)90030-1

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

[No abstract available]

引用

页码：339 / 349

页数：11

共 47 条

[1] 2 NOVEL HEAT-SHOCK GENES ENCODING PROTEINS PRODUCED IN RESPONSE TO HETEROLOGOUS PROTEIN EXPRESSION IN ESCHERICHIA-COLI [J].

ALLEN, SP ;

POLAZZI, JO ;

GIERSE, JK ;

EASTON, AM .

JOURNAL OF BACTERIOLOGY, 1992, 174 (21) :6938-6947

[2]

Arrigo A.P., 1994, BIOL HEAT SHOCK PROT, P335

[3]

Ausubel F. M., 1995, SHORT PROTOCOLS MOL, P21

[4] SUPRAMOLECULAR STRUCTURE OF THE RECOMBINANT MURINE SMALL HEAT-SHOCK PROTEIN HSP25 [J].

BEHLKE, J ;

LUTSCH, G ;

GAESTEL, M ;

BIELKA, H .

FEBS LETTERS, 1991, 288 (1-2) :119-122

[5] THE SMALL HEAT-SHOCK PROTEIN HSP26 OF SACCHAROMYCES-CEREVISIAE ASSEMBLES INTO A HIGH-MOLECULAR-WEIGHT AGGREGATE [J].

BENTLEY, NJ ;

FITCH, IT ;

TUITE, MF .

YEAST, 1992, 8 (02) :95-106

[6] ALPHA-B SUBUNIT OF LENS-SPECIFIC PROTEIN ALPHA-CRYSTALLIN IS PRESENT IN OTHER OCULAR AND NON-OCULAR TISSUES [J].

BHAT, SP ;

NAGINENI, CN .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1989, 158 (01) :319-325

[7]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[8]

BUCHNER J, 1998, METHOD ENZYMOL, V290, pCH27

[9] Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation [J].

Chang, ZY ;

Primm, TP ;

Jakana, J ;

Lee, IH ;

Serysheva, I ;

Chiu, W ;

Gilbert, HF ;

Quiocho, FA .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (12) :7218-7223

[10] THE APPARENT MOLECULAR-SIZE OF NATIVE ALPHA-CRYSTALLIN-B IN NONLENTICULAR TISSUES [J].

CHIESA, R ;

MCDERMOTT, MJ ;

MANN, E ;

SPECTOR, A .

FEBS LETTERS, 1990, 268 (01) :222-226

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