[28] Enzymatic deglycosylation of glycoproteins

作者: Nageswara R. Thotakura , Om P. Bahl

DOI: 10.1016/0076-6879(87)38030-9

关键词: Native stateCleaveFunction (biology)ChemistryEnzymeHydrolysisSubstrate (chemistry)GlycoproteinBiochemistryBiosynthesis

摘要: Publisher Summary Deglycosylation of glycoproteins is important in elucidation structure, function, and biosynthesis biologically significant glycoproteins. Enzymatic deglycosylation can be brought about by exoglycosidases either used sequentially or a mixture endoglycosidases. The chapter discusses the conditions processes Denatured are more susceptible to hydrolysis with these enzymes than their native conformation. Complete conformation can, however, achieved using much higher concentrations enzyme. precise for including enzyme concentration incubation time vary substrate and, therefore, should determined each unknown glycoprotein separately. Despite discovery several endoglycosidases that have facilitated investigations on structure carbohydrates, there still remains paucity broad specificity cleave carbohydrates from forms. There need continue efforts search new endoenzymes.

参考文章(15)
WR Moyle, OP Bahl, L März, Role of carbohydrate of human chorionic gonadotropin in the mechanism of hormone action. Journal of Biological Chemistry. ,vol. 250, pp. 9163- 9169 ,(1975) , 10.1016/S0021-9258(19)40704-7
Premanand V. Wagh, Om P. Bahl, Alan D. Elbein, Sugar Residues on Protein Critical Reviews in Biochemistry. ,vol. 10, pp. 307- 377 ,(1981) , 10.3109/10409238109113602
J. Umemoto, V.P. Bhavanandan, E.A. Davidson, Purification and properties of an endo-alpha-N-acetyl-D-galactosaminidase from Diplococcus pneumoniae. Journal of Biological Chemistry. ,vol. 252, pp. 8609- 8614 ,(1977) , 10.1016/S0021-9258(19)75264-8
T H Plummer, J H Elder, S Alexander, A W Phelan, A L Tarentino, Demonstration of peptide:N-glycosidase F activity in endo-beta-N-acetylglucosaminidase F preparations. Journal of Biological Chemistry. ,vol. 259, pp. 10700- 10704 ,(1984) , 10.1016/S0021-9258(18)90568-5
Anthony L. Tarentino, Frank Maley, Purification and Properties of an Endo-β-N-acetylglucosaminidase from Streptomyces griseus Journal of Biological Chemistry. ,vol. 249, pp. 811- 817 ,(1974) , 10.1016/S0021-9258(19)43001-9
J M Goverman, T F Parsons, J G Pierce, Enzymatic deglycosylation of the subunits of chorionic gonadotropin. Effects on formation of tertiary structure and biological activity. Journal of Biological Chemistry. ,vol. 257, pp. 15059- 15064 ,(1982) , 10.1016/S0021-9258(18)33393-3
P W Robbins, R B Trimble, D F Wirth, C Hering, F Maley, G F Maley, R Das, B W Gibson, N Royal, K Biemann, Primary structure of the Streptomyces enzyme endo-beta-N-acetylglucosaminidase H. Journal of Biological Chemistry. ,vol. 259, pp. 7577- 7583 ,(1984) , 10.1016/S0021-9258(17)42829-8