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Heat shock response in Neurospora crassa: purification and some properties of HSP 80.

作者信息

Roychowdhury H S, Kapoor M

机构信息

Department of Biological Sciences, University of Calgary, Alta., Canada.

出版信息

Biochem Cell Biol. 1990 Oct;68(10):1218-21. doi: 10.1139/o90-180.

DOI:10.1139/o90-180
PMID:2148482
Abstract

The heat shock response of Neurospora crassa was investigated. A 80-kilodalton heat shock protein (HSP 80) was purified to near homogeneity from heat-shocked mycelial extracts employing ammonium sulphate fractionation, gel filtration, and ion-exchange and affinity chromatography. It was observed to migrate as a single band on one-dimensional sodium dodecyl sulphate--polyacrylamide gels, with a molecular mass of approximately 83 kilodaltons (kDa). On two-dimensional gels it resolved into four polypeptide species with isoelectric points in the acidic range, which on staining with periodic acid--Schiff method were demonstrated to be glycosylated. In the native state, HSP 80 had a molecular size of approximately 610 kDa.

摘要

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