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B P Chatterjee

Publications and source records attributed to B P Chatterjee.

At least 37 records · Page 2Linked to original sources
PubMed1991

Studies on the effect of various parameters on crotalarin-fetuin interaction.

With a view to optimise the interaction of crotalarin, a blood group A-specific lectin from the seeds of Crotalaria striata with fetuin the effect of various parameters on the reaction has been studied turbidimetrically. The formation of crotalarin-fetuin complex was dependent on time, temperature, pH and the ionic strength of the medium. The maximum turbidity appeared in 30 min at 20 degrees C and the pH optimum was 3.5. The binding constant (Ka) for crotalarin-fetuin interaction was 5.58 x 10(4) M-1 (pH 3.5) at 20 degrees C. Among the different inorganic salts tested, the cations with increasing concentrations had pronounced effect on binding. KCNS and KI, however, were noninhibitory. The turbidity slightly increased in presence of different sodium salts, whereas periodate and urea reduced the interaction. The different alcohols had no remarkable effect on the above reaction.

Hydrogen-Ion Concentration↗
PubMed1990

Chemical modification studies on a blood group A-specific lectin, crotalarin (Crotalaria striata) and its effect on hemagglutinating activity.

Crotalarin, the N-acetyl-D-galactosamine-binding blood group A-specific lectin from the seeds of Crotalaria striata was subjected to various chemical modifications in order to ascertain the amino acid residues responsible for its carbohydrate-binding property. Modification of lysine, cysteine and arginine residues did not affect the carbohydrate-binding activity of the lectin. However, modification of tyrosine residue and carboxy group of the acidic amino acids led to a complete loss of its activity, indicating the involvement of tyrosine and aspartic and glutamic acid in the saccharide-binding respectively. The hemagglutinating activity of the lectin was completely/almost completely lost by modification of tryptophan residues. The relative loss in hemagglutinating activity on modification of tryptophan residues indicate that one residue/molecule is required for the carbohydrate-binding activity of the lectin. Modification was not effective in the presence of D-galactose (0.2 M). A marked decrease in the fluorescence emission was found as the tryptophan residues of crotalarin were modified. The c.d. spectra showed the presence of an identical pattern of conformation in the native and modified lectins which confirms that the loss in activity was due to modification only. The effect of periodate oxidation on crotalarin showed loss of activity whereas action of enzymes retained most of the activity.

ABO Blood-Group System↗
PubMed1990

Isolation of concanavalin A-reactive low-molecular weight allergen from house dust.

A concanavalin A-reactive low-molecular weight (MW approximately 7000) glycoprotein allergen has been isolated from house dust. The crude allergen was fractionated by Sephadex gel filtration followed by separation into two allergenic components by affinity chromatography on concanavalin A-Sepharose column. The column-bound fraction contains Man (11.7%), Gal (2.34%), GlcNAc (3.47%) and a trace of Glc and has been proved to be more potent allergen for house dust-sensitive patients both in vivo and in vitro tests.

Allergens↗
PubMed1989

Further characterization and immunochemical studies on the carbohydrate specificity of jackfruit (Artocarpus integrifolia) lectin.

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.

Animals↗
PubMed1989

Lectin typing of Pseudomonas aeruginosa strains of different serogroups, Habs and Fisher types.

Sixteen Habs and three Fisher types of Pseudomonas aeruginosa were typed with lectins of know specificity resulting from their interaction with bacterial cell surface carbohydrates as evidenced by agglutination-inhibition assay with simple carbohydrates. Lipopolysaccharides of few strains of Pseudomonas are precipitated with different lectins and the results are corroborated by those of agglutination suggesting that Pseudomonas aeruginosa can be characterized intraspecifically by lectins.

Agglutination Tests↗
PubMed1988

Wistaria sinensis agglutinin: purification, carbohydrate specificity, and characterisation of the combining site.

A 2-acetamido-2-deoxy-D-galactose-binding agglutinin from Wistaria sinensis seeds, purified by affinity chromatography on a 2-acetamido-2-deoxy-D-galactose-starch conjugate, was homogeneous as judged by poly(acrylamide) disc gel electrophoresis. It had a mol. wt. of 66,000 (gel filtration on Sephadex G-150); on electrophoresis on SDS-poly(acrylamide) gel in the presence of 2-mercaptoethanol, it dissociated into sub-units of mol. wt. 34,000, suggesting the agglutinin to be a dimer; and it was a glycoprotein containing 4.8% of carbohydrate. It agglutinated several vertebrate erythrocytes, including human regardless of the blood group. In hapten-inhibition assays, 2-acetamido-2-deoxy-D-galactose and its glycosides were found to be better inhibitors than D-galactose and its glycosides, but N-acetyl-lactosamine was the most potent inhibitor. The binding involved HO-3,4 of the haptens and HO-2 partially.

Animals↗
PubMed1987

Hemagglutination patterns of Pseudomonas aeruginosa strains of different serogroups, Habs and Fisher types.

Pseudomonas aeruginosa strains of sixteen Habs and three Fisher types were examined for their hemagglutination activity using vertebrate erythrocytes including human ones. Their carbohydrate-binding specificity as determined by hemagglutination-inhibition suggests a possible method of their purification. This study also indicates the possibility of an occurrence of multiple lectins of different specificity.

Hemagglutination Inhibition Tests↗
PubMed1986

Serological characterization of humoral lectin from Heterometrus granulomanus scorpion hemolymph.

A lectin in the hemolymph of Indian scorpion Heterometrus granulomanus was detected by agglutination of human and animal erythrocytes. The agglutinating activity was enhanced in presence of Ca2+ ion. The lectin shows specificity for sialic acid like many other sialic acid-specific lectins such as "Limulin", as the agglutination of erythrocytes was completely abolished by treatment with Vibrio cholerae neuraminidase. However, neuraminidase-treated rat and mouse erythrocytes exhibited high titers. This result was substantiated by crossed-absorption test which suggests the adjunct specificity of the Heterometrus lectin for these cells. Hemagglutination-inhibition results of the lectin indicate that sialic acid including its derivatives and sialoglycoconjugates are the inhibitors among which glycophorin was most potent.

Animals↗
PubMed1986

Purification of a sialic acid-specific lectin from the Indian scorpion Heterometrus granulomanus.

A sialic acid-specific lectin, scorpin, has been purified to apparent homogeneity from the Indian scorpion Heterometrus granulomanus by affinity chromatography on equine submandibular gland glycopeptides linked to Sepharose and gel filtration on Sephadex G-200. The lectin has a molecular mass of 500 000 Da and was dissociated into single polypeptide chains of 15 000 Da, as determined by SDS gel electrophoresis in the presence of 2-mercaptoethanol. Scorpin is a glycoprotein containing 2.8% sugars. Its specificity was investigated by the inhibition of hemagglutination with various derivatives of sialic acid and other sugars. N-Acetylneuraminic acid gave better inhibition than N-glycoloylneuraminic acid but showed less inhibitory effect than sialyl-alpha(2----3)-lactose and disialyllactose. Among the sialoglycoconjugates tested, equine submandibular gland glycopeptide was found to be the most potent inhibitor. Scorpin showed a strong tendency to bind to carboxyl groups, since reduction of the carboxyl group of N-acetylneuraminic acid destroyed the inhibitory potency of this sugar. Furthermore, D-glucuronic acid inhibited hemagglutination whereas N-acetylglucosamine or N-acetylgalactosamine were not inhibitors.

Animals↗
PubMed1985

Jackfruit (Artocarpus integrifolia) and the Agaricus mushroom lectin fit also to the so-called peanut receptor.

The lectin from jackfruit (Artocarpus integrifolia) reacts with the peanut-specific lectin receptor represented by the T-disaccharide, which is also part of the Thomsen (= T)-Friedenreich antigen, namely O-beta-D-galactosyl-(1----3)-N-acetyl-D-galactosamine. The difference between the jackfruit lectin and peanut lectin has been shown to be mainly due to the further linkage of the T-disaccharide: Whereas the peanut lectin reacts with both anomeric forms, jackfruit lectin and the closely - with respect to its specificity - related Agaricus bisporus mushroom lectin react predominantly with the alpha-linked T-disaccharide, so that they cannot detect the lipid-linked T-disaccharide, as the peanut lectin does.

Antigens, Tumor-Associated, Carbohydrate↗
PubMed1978

Additional precipitation reactions of lectins with human serum glycoproteins.

Highly purified human serum glycoproteins were treated with neuraminidase and examined for their cross reaction with several lectins with anti-galactosyl specificity: beta-D-galactosyl structures are thought to be the main terminal sugar residues that become attached de novo after removal of neuraminic acid. The following lectins were tested: Tridacnin from the bivalve clams Tridacna maxima and Tridacna gigas, the agglutinin from the sponge Axinella polypoides, the lectin from the roach Rutilus rutilus and the plant lectins from Ricinus communis, Ononis spinosa, Glycine soja and Abrus precatorius. In agar gel diffusion, these purified and precipitating lectins gave more or less strong or negative results against the different neuraminidase-treated serum glycoproteins, thus indicating subtle differences with respect to their anti-galactosyl combining specificity. On the other hand, serum glycoproteins which reacted with the same lectin, did not always show complete identity lines. Finally, as revealed by these lectins, the carbohydrate moiety of serum glycoproteins may reflect a complex and broad spectrum of heterogeneity. This could lead to a more detailed understanding of the topographical and steric arrangement of the chemical structure and of the biological role of carbohydrate groups in these glycosubstances.

Animals↗
PubMed1978

A new group of mitogenic lectins from invertebrate sources.

In the haemolymph of the Tridacnid bivalve clams anti-galactans occur which do not have only glycosubstance precipitating and cell agglutinating properties, but also show mitogenic activity with respect to the blast transformation of human peripheral lymphocytes. This new property can be inhibited in a specific way by galactans and is destroyed by the degradation of the mitogenic lectin into subunits by polymer bound pronase. Quite a number of invertebrate haemolymph samples and snail albumin gland extracts, containing agglutinin activity, proved to have no mitogenic potency. The only exception was found in an extract of the snail albumin gland of Ampullaria canaliculata which contained a strong mitogen of the lectin type.

Agglutinins↗
PubMed1976

Spinal cysticercosis.

Cysticercosis of the spinal cord is rare. A case is reported in a 40-year-old Hindu. Compression of the spinal cord by the cyst which was located in the arachnoid membrane resulted in a paraplegia. Removal of the cyst resulted in marked improvement.

Adult↗