ISSN:
1573-4986
Keywords:
Deglycosylation
;
endoglycosidase F
;
acute-phase protein
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Endo-β-N-acetylglucosaminidase F (endo F, EC 3.2.1.96) and peptide:N-glycosidase F (PNGase F, EC 3.2.2.18) fromFlavobacterium meningosepticum were used for the deglycosylation of α1-proteinase inhibitor and α1-acid glycoprotein carrying oligosaccharide side chains of the complex-, high-mannose- and hybrid-type. High-mannose-and hybrid-type glycoproteins were obtained by the incubation of rat hepatocyte primary cultures with 1-deoxymannojirimycin or swainsonine, respectively. It was found that endo F cleaves hybrid- and high-mannose-type α1-proteinase inhibitor and α1-acid glycoprotein at pH 4.5 as well as at pH 8.5 in the presence or absence of 1% octyl-β-d-glucopyranoside. Complex-type α1-proteinase inhibitor or α1-acid glycoprotein were not cleaved by endo F even in the presence of octyl-β-d-glucopyranoside. PNGase F was found to cleave complex-, hybrid- and high-mannose-type oligosaccharide side chains of α1-proteinase inhibitor and α1-acid glycoprotein at pH 4.5 and pH 8.5 in the presence of 0.75% octyl-β-d-glucopyranoside. The deglycosylation of both protein substrates was very poor without detergents.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01051775
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