caa a22 4500 397557779 CHVBK 20180308164807.0 cr unu---uuuuu 161202e199605 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021341 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021341 Purification and Characterization of Hen Oviduct αl,2-Mannosidase [Elektronische Daten] [Noriko Hamagashira, Hisashi Oku, Tomohiro Mega, Sumihiro Hase] An a-mannosidase capable of hydrolyzing three Man αl,2-residues from pyridylamine-(PA-) labeled Man9GlcNAc2 was purified from hen oviduct. The purity of the preparation was analyzed by PAGE; its molecular weight was 42,000 by SDS-PAGE or 50,000 by gel filtration. The pH optimum was 6.5. The enzyme was inactivated with EDTA; enzyme activity was restored by the addition of Ca2+. The enzyme acitivity was inhibited by 1-deoxymannojirimycin, but not by swainsonine. The substrate specificity of the purified enzyme was analyzed using PA-oligomannose-type sugar chains. When Man9GlcNAc2-PA was digested, Manαl-6(Manαl-2Manαl-3)Manαl-6(Manαl-3)Manβl-4GlcNAc;β1-4Glc-NAc-PA was obtained as an end product, and the enzyme was incapable of hydrolyzing p-nitrophenyl α-D-mannoside and Man αl,3- or Man α,6-residues. Judging from these characteristics, the enzyme was classified as a Man2-mannosidase or Golgi mannosidase I and speculated to participate in the processing or catabolism of glycoproteins. © by the Journal of Biochemistry Regular Papers nationallicence αl nationallicence 2-mannosidase nationallicence Ca2+-dependent enzyme nationallicence Golgi mannosidase I nationallicence hen oviduct nationallicence Man9 -mannosidase nationallicence Hamagashira Noriko Department of Chemistry, Osaka University College of Science, Toyonaka, Osaka 560 aut Oku Hisashi Department of Chemistry, Osaka University College of Science, Toyonaka, Osaka 560 aut Mega Tomohiro Department of Chemistry, Osaka University College of Science, Toyonaka, Osaka 560 aut Hase Sumihiro Department of Chemistry, Osaka University College of Science, Toyonaka, Osaka 560 aut The Journal of Biochemistry Oxford University Press 119/5(1996-05), 998-1003 0021-924X 119:5<998 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021341 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021341 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Hamagashira Noriko Department of Chemistry, Osaka University College of Science, Toyonaka, Osaka 560 aut NATIONALLICENCE 700 1- Oku Hisashi Department of Chemistry, Osaka University College of Science, Toyonaka, Osaka 560 aut NATIONALLICENCE 700 1- Mega Tomohiro Department of Chemistry, Osaka University College of Science, Toyonaka, Osaka 560 aut NATIONALLICENCE 700 1- Hase Sumihiro Department of Chemistry, Osaka University College of Science, Toyonaka, Osaka 560 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/5(1996-05), 998-1003 0021-924X 119:5<998 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford