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Properties of the lectin from the hog peanut (Amphicarpaea bracteata).

Abstract：

:An N-acetyl-D-galactosamine-specific lectin has been isolated from the two seed forms of the hog peanut (Amphicarpaea bracteata) using an affinity support containing the synthetic type A blood group trisaccharide alpha-D-GalNAc-(1,3)-[alpha-L-Fuc-(1,2)]-beta-D-Gal (Synsorb A). The affinity-purified lectin appears to be identical in both seed types. Gel filtration on Sephadex G-200 gives a single symmetrical peak corresponding to Mr 135,000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis shows four subunit forms, each of which contains carbohydrate. Limited amino terminal sequencing indicates heterogeneity in two of the first 10 residues. The lectin contains no cysteine. There are four equivalent, noninteracting GalNAc binding sites per 135,000-Da molecule, having an association constant for methyl N-acetyl-alpha-D-galactosaminide of 4.0 X 10(4) M-1. Precipitin and hapten inhibition studies show the lectin to be specific for terminal, nonreducing D-GalNAc units, with a preference for the alpha-anomer and enhanced specificity for the disaccharide, GalNAc alpha 1,3GalNAc. There is also a single adenine binding site per Mr 135,000 lectin molecule with an association constant of 1.3 X 10(6) M-1.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Maliarik MJ,Roberts DD,Goldstein IJ

doi

10.1016/0003-9861(87)90310-9

subject

Has Abstract

pub_date

1987-05-15 00:00:00

pages

194-200

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(87)90310-9

journal_volume

255

pub_type

杂志文章

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