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PURIFICATION AND PARTIAL CHARACTERIZATION OF A LECTIN FROM THE SEEDS OF DIOCLEA GUIANENSIS 1
Author(s) -
VASCONCELOS ILKA MARIA,
CAVADA BENILDO SOUSA,
MOREIRA RENATO DE AZEVEDO,
OLIVEIRA JOSE TADEU ABREU DE
Publication year - 1991
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1991.tb00150.x
Subject(s) - lectin , affinity chromatography , biochemistry , chemistry , threonine , sephadex , aspartic acid , chromatography , carbohydrate , polyacrylamide gel electrophoresis , amino acid , concanavalin a , serine , sepharose , biology , enzyme , in vitro
A lectin was purified from seeds of Dioclea guianensis by Sephadex G‐50 affinity chromatography. Apparent homogeneity of the lectin was demonstrated by native polyacrylamide gel electrophoresis, chromatography on DEAE‐ and CM‐Sepharose, and immunochemistry. The lectin showed a carbohydrate specificity for D‐mannose (D‐glucose)‐binding, had a requirement for Ca −2 and Mn −2 , contained no covalently bound carbohydrate and had an amino acid composition characterized by high content of aspartic acid, serine and threonine, and low levels of sulfur‐containing amino acids. At pH 7.5 it exists as two species of molecular weight about 100 and 47 kD and in dissociating solvents three subunits of approximate size of 30, 18 and 12 kD were obtained. The lectin agglutinated erythocytes from rabbit and chicken but not from human, cow, sheep, goat or pig and was toxic to brine shrimp (Artemia salina) larvae. It was relatively heat‐stable, retaining half of its original activity even after 90 min at 70°C.