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 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.
Roychowdhury
H S
HS
Department of Biological Sciences, University of Calgary, Alta., Canada.
Kapoor
M
M
D005656:Fungal Proteins / Q000302:isolation & purification*; D006360:Heat-Shock Proteins / Q000302:isolation & purification* / Q000502:physiology; D006358:Hot Temperature; D008970:Molecular Weight; D009492:Neurospora crassa / Q000032:analysis / Q000502:physiology*; D013329:Structure-Activity Relationship
D005656:Fungal Proteins; D006360:Heat-Shock Proteins