title: [The protein spectrum and thermostability of the lysosomal hydrolases in heat-resistant sublines of Chinese hamster cells].
abstract: It has been shown by electrophoresis that the earlier obtained thermoresistant sublines of the CHO-K1 cell line do not accumulate heat shock proteins when cultured at 37 degrees C. The thermostability of two lysosomal proteins--acid lipase and acid phosphatase--were higher in the thermoresistant cells than in the parental cells, whereas no differences in thermostability of galactosidase were found between heat resistant and parental lines. Thus, it is concluded that changes in the level of conformational flexibility of protein molecules may be one of the mechanisms of cell adaptation to growth at higher temperatures.
authors.forename: M F
authors.initials: MF
authors.lastname: Konstantinova
authors.forename: A N
authors.initials: AN
authors.lastname: Bogomazova
authors.forename: T N
authors.initials: TN
authors.lastname: Beliaeva
authors.forename: A G
authors.initials: AG
authors.lastname: Bulychev
authors.forename: E A
authors.initials: EA
authors.lastname: Leont'eva
mesh_terms: D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D003412:Cricetulus; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D005260:Female; D006360:Heat-Shock Proteins / Q000032:analysis / Q000378:metabolism*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D006867:Hydrolases / Q000032:analysis / Q000378:metabolism*; D008247:Lysosomes / Q000201:enzymology*; D010053:Ovary
chemical_list: D006360:Heat-Shock Proteins; D006867:Hydrolases