The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Structures of the carbohydrate moiety of ovalbumin glycopeptide III and the difference in specificity of endo-beta-N-acetylglucosaminidases CII and H.
Open accessAbstract
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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Citations
Cites
Purification and Properties of an Endo-β-N-acetylglucosaminidase from Streptomyces griseus
Tarentino, A. L., & Maley, F. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43001-9 · Cited by 850
Goldstein, I. J., Hollerman, C. E., & Smith, E. E. (1965) · Biochemistry · doi:10.1021/bi00881a013 · Cited by 850
Determination of aminosugar linkages in glycolipids by methylation
Stellner, K., Saito, H., & Hakomori, S.-I. (1973) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(73)90138-0 · Cited by 830
Comparative Aspects of Glycoprotein Structure
Kornfeld, R., & Kornfeld, S. (1976) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.45.070176.001245 · Cited by 760
Tai, T., Yamashita, K., Ogata-Arakawa, M., Koide, N., Muramatsu, T., Iwashita, S., Inoue, Y., & Kobata, A. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40797-7 · Cited by 431
Self-citation[90] α-Mannosidase, β-N-acetylhexosaminidase, and β-galactosidase from jack bean meal
Li, Y.-T., & Li, S.-C. (1972) · Methods in Enzymology · doi:10.1016/0076-6879(72)28094-6 · Cited by 405
[12] Methylation analysis of polysaccharides
Lindberg, B. (1972) · Methods in Enzymology · doi:10.1016/0076-6879(72)28014-4 · Cited by 360
Method for Fingerprinting Yeast Cell Wall Mannans
Kocourek, J., & Ballou, C. E. (1969) · Journal of Bacteriology · doi:10.1128/jb.100.3.1175-1181.1969 · Cited by 339
Microheterogeneity and paucidispersity of glycoproteins
Huang, C.-C., Mayer, H. E., & Montgomery, R. (1970) · Carbohydrate Research · doi:10.1016/s0008-6215(00)84902-2 · Cited by 277
Endo-β-N-acetylglucosaminidase Acting on Carbohydrate Moieties of Glycoproteins
Koide, N., & Muramatsu, T. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42406-x · Cited by 267
Cited by
The complete amino-acid sequence of hen ovalbumin
NISBET, A. D., SAUNDRY, R. H., MOIR, A. J. G., FOTHERGILL, L. A., & FOTHERGILL, J. E. (1981) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1981.tb05243.x · Cited by 470
Crystal structure of uncleaved ovalbumin at 1·95 Å resolution
Stein, P. E., Leslie, A. G. W., Finch, J. T., & Carrell, R. W. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)80185-w · Cited by 426
A Novel Human Serum Lectin with Collagen- and Fibrinogen-like Domains That Functions as an Opsonin
Matsushita, M., Endo, Y., Taira, S., Sato, Y., Fujita, T., Ichikawa, N., Nakata, M., & Mizuochi, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.5.2448 · Cited by 329
Li, E., & Kornfeld, S. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)46950-0 · Cited by 91
Metadata
- Authors
- Tai, T., Yamashita, K., Ito, S., & Kobata, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1977-10
- Volume
- 252
- Issue
- 19
- Pages
- 6687-6694
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1625540616
- Cited by
- 276
- References
- 14
- FWCI
- 6.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Tai, T., Yamashita, K., Ito, S., & Kobata, A. (1977). Structures of the carbohydrate moiety of ovalbumin glycopeptide III and the difference in specificity of endo-beta-N-acetylglucosaminidases CII and H. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)39903-9
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