The relationship between different forms of human alpha-mannosidase.
The tissue distribution and some properties of human alpha-mannosidase (alpha-D-mannoside mannohydrolase EC 3.2.1.24) have been studied. The acidic forms of the enzyme were fairly stable, whereas the neutral forms easily lost enzymic activity. The acidic forms were sensitive to neuraminidase but the neutral forms were unaffected. The experiments indicate that the acidic components are closely related to each other, differing only in sialic acid content and possibly conformation. The neutral forms of the enzyme are probably quite different from the acidic forms both in structure and cellular function.
D001921:Brain / Q000201:enzymology; D003016:Clostridium perfringens / Q000201:enzymology; D003035:Cobalt / Q000494:pharmacology; D004186:Disaccharidases / Q000378:metabolism*; D004355:Drug Stability; D005260:Female; D006358:Hot Temperature; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008198:Lymph Nodes / Q000201:enzymology; D008345:Manganese / Q000494:pharmacology; D008361:Mannosidases / Q000378:metabolism*; D009439:Neuraminidase; D009928:Organ Specificity; D010179:Pancreas / Q000201:enzymology; D010920:Placenta / Q000201:enzymology; D011247:Pregnancy; D013154:Spleen / Q000201:enzymology
D007527:Isoenzymes; D003035:Cobalt; D008345:Manganese; D004186:Disaccharidases; D008361:Mannosidases; D009439:Neuraminidase