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    Please use this identifier to cite or link to this item: http://tkuir.lib.tku.edu.tw:8080/dspace/handle/987654321/61590

    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:[化學學系暨研究所] 期刊論文

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