Endo-β-N-acetylglucosaminidase from fig latex

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Title:	Endo-β-N-acetylglucosaminidase from fig latex
Authors:	Chien, Su-Fang;Weinburg, Robin;Li, Su-Chen;Li, Yu-Teh
Contributors:	淡江大學化學學系
Date:	1977-01
Issue Date:	2013-05-31 11:34:45 (UTC+8)
Publisher:	Maryland Heights: Academic Press
Abstract:	Commercially available fig latex contains several endo-β-N-acetylglucosaminidases which catalyze the reaction: (Man)nG1cNAcβ1→4G1cNAcAsn → (Man)nG1cNAc + G1cNAcAsn. Using (NH4)2SO4 fractionation followed by chromatography on Sephadex G-100 and DEAE-Sephadex A-50, two distinct types of endo-β-N-acetylglucosaminidases have been partially purified and characterized. One, called F-I, hydrolyzes the di-N-acetylchitobiosyl linkage in the glycopeptide, (Man)3(G1cNAc)2Asn prepared from human IgG, much faster than that linkage in the glycopeptides, (Man)5(G1cNAc)2Asn and (Man)6(G1cNAc)2Asn both from ovalbumin. The other, called F-II, hydrolyzes the same linkage in (Man)5(G1cNAc)2-Asn and (Man)6(G1cNAc)2Asn, but not that in (Man)3(G1cNAc)2Asn.
Relation:	Biochemical and Biophysical Research Communications 76(2), pp.317-323
DOI:	10.1016/0006-291X(77)90727-6
Appears in Collections:	[Graduate Institute & Department of Chemistry] Journal Article

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