title: Characterization of high-molecular-mass heat shock proteins and 42 degrees C-specific heat shock proteins of murine cells.
abstract: There are two isoforms of high-molecular-mass heat shock protein (HMM-HSP), hsp105A and hsp105B, in murine FM3A cells. To characterize the HMM-HSPs, we here purified hsp105A and hsp105B, as well as 42 degrees C-specific HSPs that are specifically induced by continuous heating at 42 degrees C, from the cytoplasmic extracts of the FM3A cells heat-shocked at 42 degrees C for 8 h. Digestion of the hsp105A, hsp105B, and 42 degrees C-specific HSPs with lysyl endopeptidase generated 17,000-Da polypeptide fragments in common, and the N-terminal amino acid sequences of the fragments revealed a homology with those of the adenosine binding domain of hsp70 family proteins and actin. Thus, the two isoforms of hsp105 and the 42 degrees C-specific HSPs seemed to be very similar proteins having a ATP binding domain in common, and these HSPs may constitute a HMM-HSP family in murine cells.
authors.affiliation: Department of Biochemistry, Kyoto Pharmaceutical University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Hatayama
authors.forename: K
authors.initials: K
authors.lastname: Yasuda
authors.forename: E
authors.initials: E
authors.lastname: Nishiyama
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D002845:Chromatography; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D006360:Heat-Shock Proteins / Q000096:biosynthesis* / Q000737:chemistry* / Q000302:isolation & purification; D006358:Hot Temperature; D006801:Humans; D007525:Isoelectric Focusing; D008715:Methionine / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010449:Peptide Mapping; D017386:Sequence Homology, Amino Acid; D013462:Sulfur Radioisotopes
chemical_list: D006360:Heat-Shock Proteins; D013462:Sulfur Radioisotopes; D017886:Durapatite; D008715:Methionine