Characterization of purified avian 90,000-Da heat shock protein.

Abstract:

:The so-called 90,000-Da heat shock protein (hsp90) from chicken liver has been purified and physically characterized in the presence of high levels of the serine phosphatase inhibitor fluoride. The protein is an elongated dimer with a molecular weight of 160,000 and a frictional ratio of 1.6. On two-dimensional electrophoresis it exhibits several isoelectric forms lying between pH 5.1 and 5.8. It contains an average of 5.8 mol of covalently bound phosphate per dimer and is thus extensively phosphorylated. Analysis of the ultraviolet spectrum showed the purified protein to be free of nucleotide-containing components. Molybdate has been shown to stabilize complexes between the 90,000-Da heat shock protein and steroid receptors. However, molybdate has no effect on the sedimentation of the purified heat shock protein. Proteins structurally related to hsp90 have been reported to penetrate the endoplasmic reticulum. However, when purified hsp90 was tested using the partition method of Bordier, which distinguishes hydrophilic and lipophilic proteins, it partitioned totally into the aqueous phase.

journal_name

Arch Biochem Biophys

authors

Iannotti AM,Rabideau DA,Dougherty JJ

doi

10.1016/0003-9861(88)90569-3

subject

Has Abstract

pub_date

1988-07-01 00:00:00

pages

54-60

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(88)90569-3

journal_volume

264

pub_type

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