scholarly journals Isolation and partial characterization of a lectin from Euphorbia heterophylla seeds

1983 ◽  
Vol 215 (1) ◽  
pp. 141-145 ◽  
Author(s):  
M Nsimba-Lubaki ◽  
W J Peumans ◽  
A R Carlier
Keyword(s):  
Affinity Chromatography ◽  
Partial Characterization ◽  
Dimeric Protein

An N-acetylgalactosamine-specific lectin was isolated from Euphorbia heterophylla seeds by affinity chromatography on cross-linked arabinogalactan. It is a dimeric protein of two identical subunits of Mr 32 000, and differs structurally from all previously known Euphorbiaceae lectins. Its distribution over the seed is typical in that it is merely confined to the primary axes.

scholarly journals Isolation and partial characterization of a lectin from a false brome grass (Brachypodium sylvaticum)

1982 ◽  
Vol 205 (3) ◽  
pp. 635-638 ◽  
Author(s):  
W J Peumans ◽  
C Spaepen ◽  
H M Stinissen ◽  
A R Carlier
Keyword(s):  
Physicochemical Properties ◽  
Affinity Chromatography ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Partial Characterization ◽  
Grass Species ◽  
Brachypodium Sylvaticum ◽  
Dimeric Protein ◽  
Brome Grass

A lectin has been isolated from embryos of a false brome grass species (Brachypodium sylvaticum) by affinity chromatography on immobilized N-acetylglucosamine. It is a dimeric protein of two identical subunits of mol.wt. 18 000. Although it resembles cereal lectins with respect to its biochemical and physicochemical properties, it differs structurally in several aspects from wheat-germ-agglutinin-like lectins.

scholarly journals Purification and partial characterization of cathepsin D from porcine (Sus scrofa) liver using affinity chromatography

IUBMB Life ◽  
1998 ◽  
Vol 45 (4) ◽  
pp. 797-803 ◽  
Author(s):  
Femanda Canduri ◽  
Richard Ward ◽  
Walter de Azevedo ◽  
Roseli Gomes ◽  
R. K. Arni
Keyword(s):  
Affinity Chromatography ◽  
Cathepsin D ◽  
Sus Scrofa ◽  
Partial Characterization

scholarly journals Partial Characterization of Hog Renin Purified by Affinity Chromatography

1976 ◽  
Vol 64 (2) ◽  
pp. 621-627 ◽  
Author(s):  
Claudine DEVAUX ◽  
Joel. MENARD ◽  
Philippe SICARD ◽  
Pierre CORVOL
Keyword(s):  
Affinity Chromatography ◽  
Partial Characterization

scholarly journals Isolation and partial characterization of wheat-germ-agglutinin-like lectins from rye (Secale cereale) and barley (Hordeum vulgare) embryos

1982 ◽  
Vol 203 (1) ◽  
pp. 239-243 ◽  
Author(s):  
Willy J. Peumans ◽  
Hetty M. Stinissen ◽  
Albert R. Carlier
Keyword(s):  
Hordeum Vulgare ◽  
Affinity Chromatography ◽  
Secale Cereale ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Partial Characterization ◽  
Immunological Properties

Lectins have been isolated from embryos of Secale cereale (rye) and Hordeum vulgare (barley) by affinity chromatography on immobilized N-acetylglucosamine. Both lectins are dimeric proteins of two identical subunits of mol.wt. 18000. They resemble strongly wheat-germ agglutinin with respect to their chemical, physical, biological and immunological properties.

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