J. Biochem, 1976, Vol. 80, No. 1 1-8
© 1976 Japanese Biochemical Society
research-article |
Partial Purification and Characterization of an Endo-
-N-acetylgalactosaminidase from the Culture Medium of Diplococcus pneumoniae1
Department of Biochemistry, Kobe University School of Medicine Ikuta-ku, Kobe, Hyogo 650
The culture medium of Diplocuccus pneumoniae contains enzymic activity that cleaves Galß1
3GalNAc from desialized human erythrocyte membrane glycoprotein. The enzyme was purified 180-fold by ammonium sulfate fractionation, gel filtration through a Sephadex G-200 column, and DEAE A-25 Sephadex chromatography. The purified enzyme liberates Galß13GalNAc from glycopeptides and glycoproteins with Galß13GalNAc
lSer and Thr moieties.
The optimum pH of this enzyme is 6.0. Using glycopeptides obtained by trypsin digestion of human erythrocyte membrane glycoprotein as a substrate, a Km of 0.020 mM (on the basis of the amount of Galß13GalNAc residues) was obtained.
So far, the enzyme appears to have a strict specificity for Galß13GalNAclSer and Thr structures, because no oligosaccharides larger than trisaccharides were liberated from porcine submaxillary mucin.
1 This work has been supported by research grants from the Scientific Research Fund (1975–1976) of the Ministry of Education, Science and Culture, of Japan. This paper is taken from the dissertation submitted by Yoshinori Endo to Kobe University School of Medicine as a requirement for the degree of Doctor of Medical Science.
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