Intracellular and extracellular alpha-D-mannosidase activity of cultured skin fibroblasts: relationship to cystic fibrosis.
Fibroblast intracellular alpha-D-mannosidase was inactivated by 30--50% after 120 min at 50 degrees C. Separation of alpha-D-mannosidase by isoelectrofocusing and wheat germ lectin-Sepharose into neutral and acid components showed the former to be heat labile and the cause of the observed loss. Fetal calf serum acid alpha-D-mannosidase could be inactivated at 60 degrees C if kept at pH 9.0. Fibroblast extracellular alpha-D-mannosidase was inactivated by 50--70% after 120 min at 50 degrees C, reflecting the greater level of the neutral component. Control and cystic fibrosis alpha-D-mannosidase showed no difference.
D001826:Body Fluids / Q000201:enzymology*; D002478:Cells, Cultured; D003550:Cystic Fibrosis / Q000201:enzymology*; D005110:Extracellular Space / Q000201:enzymology*; D005347:Fibroblasts / Q000201:enzymology; D006358:Hot Temperature; D006801:Humans; D007424:Intracellular Fluid / Q000201:enzymology*; D007525:Isoelectric Focusing; D008361:Mannosidases / Q000032:analysis*; D012867:Skin / Q000201:enzymology*
D008361:Mannosidases