title: Two-step purification and N-terminal amino acid sequence analysis of the rat Mr 90,000 heat shock protein.
abstract: A fast and efficient method for the isolation of the rat Mr approximately 90,000 heat shock protein is presented, comprising a two-step high-performance anion-exchange and gel-permeation column chromatography. The Mr approximately 90,000 protein was purified to electrophoretic homogeneity in high yield (up to 2 mg per 10g of normal rat liver) in 4-5 h. The purified protein was recognized on protein immunoblots by monospecific rabbit antibodies raised against the rat glucocorticoid receptor-associated Mr approximately 90,000 non-ligand-binding protein. The N-terminal sequence of the first 25 amino acids of the purified protein showed a high degree of similarity with Mr approximately 90,000 heat shock proteins from calf, human, Drosophila, and yeast.
authors.affiliation: Department of Medical Nutrition, Karolinska Institute, Huddinge University Hospital, Sweden.
authors.forename: M
authors.initials: M
authors.lastname: Denis
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000917:Antibody Formation; D003600:Cytosol / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006360:Heat-Shock Proteins / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains
chemical_list: D006360:Heat-Shock Proteins