INTERACTIONS OF BOWRINGIA-MILDBRAEDII AGGLUTININ WITH COMPLEX- AND HYBRID-TYPE GLYCANS

被引：7

作者：

CHAWLA, D ^{[1
]}

ANIMASHAUN, T ^{[1
]}

HUGHES, RC ^{[1
]}

机构：

[1] NATL INST MED RES,LONDON NW7 1AA,ENGLAND

来源：

FEBS LETTERS | 1992年 / 298卷 / 2-3期

关键词：

BOWRINGIA-MILDBRAEDII AGGLUTININ; LECTIN; CARBOHYDRATE BINDING SPECIFICITY;

D O I：

10.1016/0014-5793(92)80079-V

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Affinity chromatography on Bowringia mildbraedii agglutinin (BMA) Sepharose of glycopeptides confirmed a previous report using oligosaccharides (Animashaun, T. and Hughes, R.C. (1989) J. Biol. Chem. 264, 4657-4663) that high affinity binding requires the sequence Man-alpha-1 --> 2 Man-alpha-1 --> 6 Man-alpha-1 --> 6 Man-beta-1 --> 4. However, moderate binding was still exhibited by structures lacking this sequence provided the oligosaccharide core sequence Man-alpha-1 --> 3[Man-alpha-1 --> 6]Man-beta-1 --> 4GlcNAc was present. This moderate binding was not affected by substitution with N-acetylglucosamine at C2 and C4, respectively, of the Man-alpha-1 --> 3 and Man-beta-1 --> 4 residues and BMA Sepharose should prove to be a useful tool for the isolation of bisected or non-bisected hybrid-type glycans.

引用

页码：291 / 296

页数：6

共 17 条

[1]

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[2]

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[3]

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[4]

CARVER JP, 1989, CIBA F SYMP, V145, P6