학술논문

Characterization of the Trimeric, Self-Recognizing Geodia cydonium Lectin I.
Document Type
Article
Source
European Journal of Biochemistry. 6/15/83, Vol. 133 Issue 2, p263-267. 5p. 2 Diagrams, 2 Charts, 3 Graphs.
Subject
*LECTINS
*IMMUNOGLOBULINS
*HEMAGGLUTININ
*GALACTOSE
*GLYCOSIDES
*GEL electrophoresis
*AFFINITY chromatography
*MOLECULAR weights
*PHASE partition
Language
ISSN
0014-2956
Abstract
A D-galactose-specific lectin I was extracted from the sponge Geodia cydonium and purified by affinity chromatography. The molecular weight of lectin I as determined by high-pressure liquid gel chromatography, was found to be 36 500 ± 1300. Disc gel electrophoresis in the presence and in the absence of sodium dodecyl sulfate showed that lectin I is a trimer composed of three different subunits (Mr: 13 800, 13 000 and 12 200); two of the three subunits are linked by one disulfide bond. Isoelectric focusing gave a pI of 5.6 for the native molecule and a pI of 4.4 and of 7.4 for the subunits. The three subunits carry carbohydrate side chains, composed of D-galactose (94%) and of arabinose (5%). Based on experiments with lectins, the terminal D-galactose residues are bound by β1 → 6 and/or β1 → 4 glycosidic linkages. The Geodia lectin I contains, besides two carbohydrate recognition sites, at least one receptor site for a second lectin I molecule. [ABSTRACT FROM AUTHOR]