Autor Horejsí V
Titel Properties of Ulex europaeus II lectin isolated by affinity chromatography.
Journal Biochimica et biophysica acta
Seiten Volume 577, Issue 2, Pages 389-93
Publikationsdatum -
Abstract

1. Biochim Biophys Acta. 1979 Apr 25;577(2):389-93.


Properties of Ulex europaeus II lectin isolated by affinity chromatography.


Horejsí V.


A lectin was isolated from Ulex europaeus seeds by affinity chromatography on 
affinity adsorbent prepared by copolymerization of acrylamide, N,N'-methylene 
bisacrylamide and maleylated hog stomach peptone. The lectin is homogeneous as 
judged by ultracentrifugation (s20,w = 6.4 S), electrophoretic and gel 
chromatography criteria; it contains 4.2% neutral sugar and 1.4% glucosamine. 
Its molecular weight is approx. 110,000 and the molecule consists of two 
noncovalently linked protomers which are formed by two covalently bound basic 
subunits (Mr = 30,000). The preparation contains three isolectins differing in 
the strength of interaction with specific sugars (cellobiose, 
N-acetyl-D-glucosamine) under the conditions of affinity electrophoresis. The 
lectin is non-specific with human ABO blood group system, the agglutination is 
inhibited by partial chitin hydrolysate, hog stomach peptone and high 
concentration of cellobiose.


PMID: 454654 [Indexed for MEDLINE]

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Medline Link https://pubmed.ncbi.nlm.nih.gov/454654/
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PMID/ISBN 454654
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