Structures of the carbohydrate moiety of ovalbumin glycopeptide III and the difference in specificity of endo-beta-N-acetylglucosaminidases CII and H.
Year: 1977
Type: article
Abstract: 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).
Source: Journal of Biological Chemistry
Authors: T Tai, K Yamashita, S Ito, A Kobata
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W1625540616