Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1989-7-5
pubmed:abstractText
The lectin from jackfruit (Artocarpus integrifolia) seeds has been purified by Rivanol (6,9-diamino-2-ethoxyacridine lactate) treatment. The specific activity, molecular weights of parent lectin and its subunit, its glycoprotein nature, and hemagglutination-inhibition assays suggest that this preparation is identical to that obtained by affinity chromatography on melibiose-agarose adsorbent (Ahmed, H., and Chatterjee, B. P. (1986) in Lectins, Biology, Biochemistry, Clinical Biochemistry (Bøg-Hansen, T. C., and van Driessche, E., eds) Vol. 5, pp. 125-133, Walter de Gruyter, New York). The lectin strongly agglutinates human and several animal erythrocytes. The lectin contains five isolectins of pI values 7.1, 6.85, 5.5, 5.3, and 5.1. It is thermally stable and loses its activity above 75 degrees C. The hemagglutinating activity remains unchanged in the presence of bivalent cations viz., Ca2+, Mg2+, Mn2+, etc. It is a metalloprotein. The lectin retains its activity by dialysis with acetic acid followed by EDTA. It agglutinates Ehrlich ascites cells. Equilibrium dialysis of lectin with melibiose and quenching of fluorescence of 4-methylumbelliferyl-alpha-D-galactopyranoside by the lectin show that homotetrameric jackfruit lectin has two sugar-binding sites. The lectin precipitates well several galactomannans and glycoproteins having terminal D-Gal-alpha-(1----6)- or D-Gal-beta-(1----3)-D-GalNAc residues. It hardly or does not precipitate polysaccharides having terminal D-Gal-alpha-(1----3) residues. Quantitative precipitin-inhibition studies using various haptens suggest that the -OCH2- group at C-1 and -OH groups at C-4 and partially at C-6 in the alpha-glycoside of D-galactose configuration are important for lectin-sugar interaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9365-72
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed-meshheading:2722839-Animals, pubmed-meshheading:2722839-Buffaloes, pubmed-meshheading:2722839-Carbohydrate Metabolism, pubmed-meshheading:2722839-Carbohydrates, pubmed-meshheading:2722839-Carcinoma, Ehrlich Tumor, pubmed-meshheading:2722839-Columbidae, pubmed-meshheading:2722839-Dialysis, pubmed-meshheading:2722839-Ducks, pubmed-meshheading:2722839-Goats, pubmed-meshheading:2722839-Hemagglutination Inhibition Tests, pubmed-meshheading:2722839-Humans, pubmed-meshheading:2722839-Hydrogen-Ion Concentration, pubmed-meshheading:2722839-Isoelectric Focusing, pubmed-meshheading:2722839-Lectins, pubmed-meshheading:2722839-Metals, pubmed-meshheading:2722839-Mice, pubmed-meshheading:2722839-Molecular Weight, pubmed-meshheading:2722839-Plant Lectins, pubmed-meshheading:2722839-Precipitin Tests, pubmed-meshheading:2722839-Precipitins, pubmed-meshheading:2722839-Receptors, Mitogen, pubmed-meshheading:2722839-Spectrometry, Fluorescence, pubmed-meshheading:2722839-Thermodynamics
pubmed:year
1989
pubmed:articleTitle
Further characterization and immunochemical studies on the carbohydrate specificity of jackfruit (Artocarpus integrifolia) lectin.
pubmed:affiliation
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Calcutta.
pubmed:publicationType
Journal Article