INVESTIGADORES
HERKOVITS Jorge
artículos
Título:
Purification and some characterization of a B-galactosidase binding soluble lectin from amphibian ovary
Autor/es:
FINK DE CABUTTI, N.; CARON, H.; JOUBERT, R.; ELOLA, M.; BLADIER, D. HERKOVITS J.
Revista:
FEBS LETTERS
Editorial:
ELSEVIER SCIENCE BV
Referencias:
Año: 1987 vol. 223 p. 330 - 334
ISSN:
0014-5793
Resumen:
Abstract
Soluble extracts of Bufo ovaries agglutinate sialidase-treated rabbit
erythrocytes. Unlike other amphibian lectins this agglutination activity does
not require the presence of calcium ions. It is specifically inhibited by
D-galactose and its derivatives. Thiodi-D-galactoside is the most potent
saccharide inhibitor followed by lactose and methyl-beta-D-galactoside,
respectively. D-Fucose, D-glucose and D-mannose do not inhibit the activity at
concentrations at or above 100 mM. The lectin has been purified 500-fold to
apparent homogeneity from the ovaries by salt extraction and affinity
chromatography on lactose-aminophenyl-agarose, with a yield of about 0.2%. The
molecular mass determined by gel filtration under native conditions was 30 kDa;
polyacrylamide gel electrophoresis in SDS gave a molecular mass of 15 kDa,
suggesting that the lectin is a dimer. The lectin has an isoelectric point of 40
and contains a high proportion of acidic amino acids.