Publications
Title | Abstract | Year Filter | PMID(sorted descending) Filter |
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a rapid procedure for the purification of iga1 and iga2 subclasses from normal human serum using protein g and jackfruit lectin (jacalin) affinity chromatography. | immunoglobulin a (iga) from pooled normal human sera was purified using antibody and protein g affinity chromatography and gel filtration high-pressure liquid chromatography (hplc). this high purity product was separated into iga1 and iga2 subclasses utilizing the agarose-bound lectin 'jacalin'. evaluation of product homogeneity by immunological testing confirmed greater than 95% purity. the total iga1 and iga2 recovered from sera was approximately 26% of the initial antibody present. | 1989 | 2628285 |
autoantibodies to lactate dehydrogenase in serum identified by use of immobilized protein g and immobilized jacalin, a jackfruit lectin. | in this method for identifying autoantibodies to lactate dehydrogenase (anti-lds) in serum, we used immobilized protein g to bind igg-complexed ld and immobilized jacalin to bind iga-complexed ld, leaving non-complexed ld in solution. the non-complexed ld and total ld were kinetically measured. we report results as ld bound to immobilized protein g and ld bound to immobilized jacalin. using sera demonstrating igg and iga anti-lds by immunoelectrophoresis (iep), respectively, we optimized the met ... | 1989 | 2582615 |
elimination of undesirable immunoglobulin contaminants including aggregated igg from gamma-globulin preparations by jackfruit lectin affinity chromatography. | jackfruit lectin, jacalin, has been characterized to combine with iga of only iga1 subclass but not with iga2 subclass and other immunoglobulins. however, we found in the present study that a lectin from another batch of jackfruit (jacalin-h) showed a different nature in binding reaction. jacalin-h combined with immunoglobulins of every class or subclass except monomer igg. more interestingly, the jacalin-h also combined with aggregated igg. by means of the jacalin-h affinity chromatography, we ... | 1988 | 2454765 |
jacalin: a lectin mitogenic for human cd4 t lymphocytes. | the major protein component of seeds from jackfruit is the lectin jacalin. jackfruit crude extracts are known to stimulate human lymphocytes, but the mitogenic properties of purified jacalin have not been studied in detail so far. study of the proliferative response of cell populations from normal human peripheral blood to purified jacalin showed it to be mitogenic through an interaction with lymphocytes by its lectin-binding site, as shown by inhibition by iga. jacalin failed to stimulate b cel ... | 1990 | 2372991 |
topography of the combining region of a thomsen-friedenreich-antigen-specific lectin jacalin (artocarpus integrifolia agglutinin). a thermodynamic and circular-dichroism spectroscopic study. | thermodynamic analysis of carbohydrate binding by artocarpus integrifolia (jackfruit) agglutinin (jacalin) shows that, among monosaccharides, me alpha galnac (methyl-alpha-n-acetylgalactosamine) is the strongest binding ligand. despite its strong affinity for me alpha galnac and me alpha gal, the lectin binds very poorly when gal and galnac are in alpha-linkage with other sugars such as in a- and b-blood-group trisaccharides, gal alpha 1-3gal and gal alpha 1-4gal. these binding properties are ex ... | 1990 | 2306217 |
hypoglycaemic activity of some medicinal plants in sri-lanka. | 1. investigations were carried out to determine whether aqueous extracts of osbeckia octandra, artocarpus heterophyllus and bambusa vulgaris truly possess oral hypoglycaemic activity. 2. all three plant extracts significantly lowered the fasting blood glucose level and markedly improved glucose tolerance in sprague-dawley rats. 3. a maximum hypoglycaemic activity was observed at +3 hr with o. octandra and b. vulgaris; with a. heterophyllus a maximum effect was not observed even at +5 hr. 4. the ... | 1990 | 2276596 |
structural and functional similarities of breadfruit seed lectin and jacalin. | aquous extracts from seeds of artocarpus altilis (breadfruit) and artocarpus heterophyllus (jackfruit) were compared by polyacrylamide gel electrophoresis. two bands of the same size (12 and 15 kd) as the jacalin subunits were the major components in breadfruit seed extract. they strongly reacted with anti-jacalin antibodies by western blotting. the breadfruit lectin displayed the same igal and igd precipitation specificity as jacalin in gel double diffusion experiments. it also stimulated in vi ... | 1990 | 2111454 |
iga binding lectins isolated from distinct artocarpus species demonstrate differential specificity. | the discovery of jacalin, a group of lectins from jackfruit seeds (artocarpus heterophyllus), has attracted considerable attention due to its numerous interesting immunological properties as well as its usefulness in the isolation of various serum proteins. we have further identified a similar lectin from the seeds of champedak (artocarpus integer) which we refer to as lectin-c and performed comparative studies with two types of jacalin isolated from different batches of the malaysian jackfruit ... | 1991 | 2062319 |
effect of artocarpus heterophyllus and asteracanthus longifolia on glucose tolerance in normal human subjects and in maturity-onset diabetic patients. | investigations were carried out to evaluate the effects of hot-water extracts of artocarpus heterophyllus leaves and asteracanthus longifolia whole plant material on the glucose tolerance of normal human subjects and maturity-onset diabetic patients. the extracts of both artocarpus heterophyllus and asteracanthus longifolia significantly improved glucose tolerance in the normal subjects and the diabetic patients when investigated at oral doses equivalent to 20 g/kg of starting material. | 1991 | 2056756 |
preparation and x-ray characterization of four new crystal forms of jacalin, a lectin from artocarpus integrifolia. | four new crystal forms of the anti-t lectin from jackfruit (artocarpus integrifolia) have been prepared and characterized. three of them, two monoclinic (p21, a = 59.4 a, b = 83.3 a, c = 63.5 a, beta = 107.7 degrees; c2, a = 106.1 a, b = 53.9 a, c = 128.0 a, beta = 95.0 a) and one orthorhombic (c222(1), a = 98.1 a, b = 67.3 a, c = 95.1 a) were grown with 2-methylpentan-2,4-diol (mpd) as the precipitant while the fourth, an hexagonal form (p6(1)22, a = b = 129.6 a, c = 157.9 a), was obtained in t ... | 1991 | 1942030 |
the identification of o-glycosylated precursors of insulin-like growth factor ii. | a procedure that combined ion exchange, gel permeation, and insulin-like growth factor-binding protein 3 (igf-bp-3) affinity chromatography with chromatofocusing and reversed-phase high pressure liquid chromatography was used to isolate high molecular weight precursors of human insulin-like growth factor ii (igf-ii) from acetic acid extracts of cohn fraction iv1. two precursors had isoelectric points (pi) of 5.1 and 5.4 and apparent mr values of 15,000 and 11,500, respectively. an apparent mr = ... | 1992 | 1569071 |
structural and electron-microscopic studies of jacalin from jackfruit (artocarpus integrifolia) show that this lectin is a 65 kda tetramer. | the 133-amino-acid sequences of the alpha-subunit of jacalin (a lectin from artocarpus integrifolia) and of the slightly larger alpha'-subunit were determined. the alpha'- and alpha-subunits, in the approximate ratio of 1:3, were found to be virtually identical in their primary structures, except for one valine for isoleucine substitution at position 113. although both alpha'- and alpha-chains were glycosylated, the extent of glycosylation in the alpha'-chain was much greater than that in the al ... | 1992 | 1520261 |
interaction of artocarpus lectins with human iga does not involve asparagine-linked oligosaccharide of the immunoglobulin. | in view of the controversy with respect to the interaction of jacalin with human iga2, a study was undertaken to assess the reactivity of the artocarpus heterophyllus lectin, as well as the lectin from artocarpus integer (lectin c), with subclasses of human immunoglobulin a by elisa. our data is consistent with the view that artocarpus lectins have no affinity for the iga2 immunoglobulins. in further support of the findings, we have established that n-linked oligosaccharide moieties of iga have ... | 1992 | 1417879 |