Partial characterization of intracellular and secreted glycosidases from rabbit articular chondrocytes in culture.
N-Acetyl-beta-hexosaminidase, beta-galactosidase and beta-glucuronidase activities were shown to be present in cultured rabbit articular chondrocytes. Secretion of enzyme activity seems to preferentially result in the accumulation of N-acetyl-beta-hexosaminidase. Three days after seeding, the amount of N-acetyl-beta-hexosaminidase activity found in the medium accounts for about 140% of the total N-acetyl-beta-hexosaminidase activity after complete disruption of the cell pellet. Optimal conditions of incubation time, cell numbers, substrate concentration, and pH for glycosidase activities were determined in 0.1% Triton X-100. Intracellular and secreted glycosidases have shown similar elution profiles by chromatofocusing. N-acetyl-beta-hexosaminidase exhibits two major forms which may play a role in the catabolism of glycosaminoglycans.
D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D002358:Cartilage, Articular / Q000166:cytology / Q000201:enzymology*; D002478:Cells, Cultured; D005959:Glucosidases / Q000032:analysis*; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000032:analysis; D011817:Rabbits
D007527:Isoenzymes; D000135:Acid Phosphatase; D005959:Glucosidases