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

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...

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Bibliographic Details
Published inBiochemistry and cell biology Vol. 68; no. 10; pp. 1218 - 1221
Main Authors Roychowdhury, H.S, Kapoor, M
Format Journal Article
LanguageEnglish
Published Canada 01.10.1990
Subjects
characterization
Fungal Proteins - isolation & purification
glycoproteins
heat shock proteins
heat stress
Heat-Shock Proteins - isolation & purification
Heat-Shock Proteins - physiology
Hot Temperature
Molecular Weight
Neurospora crassa
Neurospora crassa - analysis
Neurospora crassa - physiology
purification
Structure-Activity Relationship
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Summary: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.
ISSN:0829-8211
1208-6002
DOI:10.1139/o90-180