Abstract
Commercially available fig latex contains several endo-β-N-acetylglucosaminidases which catalyze the reaction: (Man) nG1cNAcβ 1→4G1cNAcAsn → (Man) nG1cNAc + G1cNAcAsn. Using (NH 4) 2SO 4 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.
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