| 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 |
| lectin extracts of champedak seeds demonstrate selective stimulation of t lymphocyte proliferation. | the effect of extracts of champedak (artocarpus integer) seed lectin on the proliferation of normal human lymphocyte was investigated. the iga1 binding lectin was demonstrated to stimulate the proliferation of human peripheral blood mononuclear cells. action of the lectin on enriched t and b cell populations demonstrated t lymphocyte specificity. the lectin was not mitogenic to b lymphocytes. optimal stimulation of proliferative response was achieved when cells were subjected to 5 days exposure ... | 1992 | 1627170 |
| 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 integer lectin on functional activity of guinea-pig complement. | the effect of artocarpus integer lectin (lectin c) on the functional activity of guinea-pig complement was investigated. purified and crude extract of lectin c from six cultivars of artocarpus integer seeds were found to consume complement and thus decreased the complement-induced haemolytic activity of sensitized sheep erythrocytes. the change in the complement-mediated haemolytic activity was significantly decreased when incubation of the lectins was performed in the presence of melibiose. the ... | 1994 | 8194855 |
| comparative analyses of iga1 binding lectins from seeds of six distinct clones of artocarpus integer. | purified lectins from seeds of six distinct clones of artocarpus integer (lectin c) were shown to be structurally and functionally similar. all lectins comprised of two types of non-covalently-linked subunits with apparent m(r) of 13,300 and 16,000. the lectins appeared to interact with several human serum proteins, with the predominance of the iga1 and c1 inhibitor molecules. interaction was not detected with iga2, igd, igg and igm. the lectin cs were also shown to precipitate monkey, sheep, ra ... | 1993 | 8490570 |
| isolation of a mannose-binding and ige- and igm-reactive lectin from the seeds of artocarpus integer. | a mannose-binding lectin, termed champedak lectin-m, was isolated from an extract of the crude seeds of champedak (artocarpus integer). on gel filtration chromatography, the lectin eluted in a single peak at elution volumes corresponding to 64 kda. sds-page showed the mannose-binding lectin to be composed of 16.8 kda polypeptides with some of the polypeptides being disulphide-linked to give dimers. when tested with all isotypes of immunoglobulins, champedak lectin-m demonstrated a selective stro ... | 1997 | 9461333 |
| effect of the mannose-binding artocarpus integer lectin on the cellular proliferation of murine lymphocytes. | the effect of the mannose-binding champedak (artocarpus integer) lectin-m on the cellular proliferation of murine lymphocytes was investigated in this study. our data demonstrated that the lectin was the main mitogenic component in the crude extract of the champedak seeds. it stimulated the proliferation of murine t cells at an optimal concentration of 2.5 microg/ml in a 3 day culture. lectin-m appeared to be a t-cell mitogen as it does not induce significant dna synthesis when cultured with spl ... | 1998 | 9845424 |
| an antimalarial stilbene from artocarpus integer. | antimalarial activity-guided study of the aerial parts of artocarpus integer led to the isolation of the prenylated stilbene, trans-4-(3-methyl-e-but-1-enyl)-3,5,2',4'-tetrahydroxystilbene with an ec50 of 1.7 micrograms/ml against plasmodium falciparum in culture. the known stilbenes, trans-4-isopentenyl-3,5,2',4'-tetrahydroxystilbene and 4-methoxy-2,2-dimethyl-6-(2-(2,4-dihydroxy)phenyl-trans-ethenyl)chromene , were also isolated. structures of these compounds were deduced on the basis of their ... | 2000 | 10897483 |
| the application of artocarpus integer seed lectin-m in the detection and isolation of selective human serum acute-phase proteins and immunoglobulins. | champedak (artocarpus integer) lectin-m is a lectin with high specificity and affinity for the core-mannosyl residues of the n-linked oligosaccharides of glycoproteins. we have studied the interaction of the champedak seed lectin with human serum glycoproteins that were resolved by 2-dimensional (2-d) gel electrophoresis. the lectin demonstrated strong interaction with haptoglobin beta chain, orosomucoid, alpha1-antitrypsin, alpha2-hs glycoprotein, transferrin, hemopexin, alpha1b-glycoprotein, a ... | 2001 | 11465670 |
| galactose-binding lectin from the seeds of champedak (artocarpus integer): sequences of its subunits and interactions with human serum o-glycosylated glycoproteins. | our group has previously reported the isolation, partial characterisation, and application of a galbeta1-3galnac- and iga1-reactive lectin from the seeds of champedak (artocarpus integer). in the present study, we have subjected the purified lectin to reverse-phase high performance liquid chromatography and sequenced its subunits. determination of the n-terminal sequence of the first 47 residues of the large subunit demonstrated at least 95% homology to the n-terminal sequence of the alpha chain ... | 2002 | 12127996 |
| raiders of the lost bark: orangutan foraging strategies in a degraded landscape. | deforestation is rapidly transforming primary forests across the tropics into human-dominated landscapes. consequently, conservationists need to understand how different taxa respond and adapt to these changes in order to develop appropriate management strategies. our two year study seeks to determine how wild sumatran orangutans (pongo abelii) adapt to living in an isolated agroforest landscape by investigating the sex of crop-raiders related to population demographics, and their temporal varia ... | 2011 | 21731636 |
| chryseobacterium artocarpi sp. nov., isolated from the rhizosphere soil of artocarpus integer. | a bacterial strain, designated utm-3(t), isolated from the rhizosphere soil of artocarpus integer (cempedak) in malaysia was studied to determine its taxonomic position. cells were gram-stain-negative, non-spore-forming rods, devoid of flagella and gliding motility, that formed yellow-pigmented colonies on nutrient agar and contained mk-6 as the predominant menaquinone. comparative analysis of the 16s rrna gene sequence of strain utm-3(t) with those of the most closely related species showed tha ... | 2014 | 24958763 |
| antityrosinase and antimicrobial activities from thai medicinal plants. | various dermatological disorders and microbial skin infection can cause hyperpigmentation. therefore, screenings for whitening and antimicrobial agents from thai medicinal plants have been of research interest. seventy-seven ethanol plant extracts were investigated for antityrosinase activity, eleven samples showed the tyrosinase inhibition more than 50 % were further preliminary screening for antimicrobial activity by agar disc diffusion and broth micro-dilution methods. artocarpus integer (thu ... | 2014 | 23835832 |
| extraction and characterization of artocarpus integer gum as pharmaceutical excipient. | natural polymers are widely used as excipients in pharmaceutical formulations. they are easily available, cheap and less toxic as compared to synthetic polymers. | 2014 | 24967778 |
| crystallization and initial x-ray diffraction analysis of a mannose-binding lectin from champedak. | mannose-binding lectin from champedak (artocarpus integer) is a homotetramer with a single-monomer molecular weight of 16 800 da. previous work has shown it to bind ige and igm, as well as being a mitogen of t cells in humans. champedak mannose-binding lectin has successfully been used to detect altered glycosylation states of serum proteins. the protein was crystallized at 293 k in space group p2(1)2(1)2(1) (unit-cell parameters a = 76.89, b = 86.22, c = 95.37 a) and the crystals diffracted to ... | 2010 | 20445267 |
| crystallization and preliminary structural studies of champedak galactose-binding lectin. | galactose-binding lectin from champedak (artocarpus integer) consists of two chains: alpha and beta (133 and 21 amino acids, respectively). it has been shown to recognize and bind to carbohydrates involved in iga and c1 inhibitor molecules. the protein was purified and crystallized at 293 k. crystals were observed in two space groups, p2(1) and p2(1)2(1)2, and diffracted to 1.65 and 2.6 a, respectively. | 2009 | 19724126 |
| artocarpus (moraceae)-gall midge pollination mutualism mediated by a male-flower parasitic fungus. | a previously undescribed pollination system involving a monoecious tree species, artocarpus integer (moraceae), pollinator gall midges, and fungi is reported from a mixed dipterocarp forest in sarawak, borneo. the fungus choanephora sp. (choanephoraceae, mucorales, zygomycetes) infects male inflorescences of a. integer, and gall midges (contarinia spp., cecidomyiinae, diptera) feed on the fungal mycelia and oviposit on the inflorescence. their larvae also feed on the mycelia and pupate in the in ... | 2000 | 10719005 |
| myrosinase-binding proteins are derived from a large wound-inducible and repetitive transcript. | several non-myrosinase proteins have been found in association with some of the myrosinases extracted from rape (brassica napus) seed. most of these proteins seemed to belong to a large family of proteins ranging in size over approximately 30-110 kda, namely the myrosinase-binding protein (mbp) family. potentially all of these mbps might be derived from a single large precursor, encoded by a 3.3-kb transcript. this transcript coded for a 99-kda glycine-rich protein with a highly repetitive struc ... | 1997 | 9057822 |