Publication | Open Access
Structures of the carbohydrate moiety of ovalbumin glycopeptide III and the difference in specificity of endo-beta-N-acetylglucosaminidases CII and H.
277
Citations
20
References
1977
Year
GlycobiologyMolecular BiologyPolysaccharideChemical BiologyEnzymatic ModificationCulture MediumBiosynthesisEndo-p-n-acetylglucosaminidase CGlycosylation.Another EnzymeBiotransformationBiochemistryOvalbumin Glycopeptide IiiCellular EnzymologyNatural SciencesEndo-beta-n-acetylglucosaminidases CiiPeptoidMicrobiologyCarbohydrate MoietyMedicineCarbohydrate-protein Interaction
Endo-P-N-acetylglucosaminidase C, isolated from the culture medium of Clostridium perfringens shows the same substrate specificity as this enzyme (2).Another enzyme, endo-p-N-acetylglucosaminidase C,, (C,, enzyme) was also purified from the culture medium of C. perfringens(2).This enzyme acts on ovalbumin glycopeptides IV, (Man),(GlcNA&Asn, and V, (Man),(GlcNA&Asn, and also on thyroglobulin unit A glycopeptide, (Man),(GlcNAc),Asn(2).In this respect, it has a similar substrate specificity as endo-P-N-acetylglucosaminidase H (H enzyme) purified from Streptomyces griseus (3, 4).
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