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  • Portland Press Ltd.  (12)
  • Biology  (12)
  • 1
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    Online Resource
    ‘FAS’t inhibition of malaria
    Portland Press Ltd. ; 2004
    In:  Biochemical Journal Vol. 384, No. 3 ( 2004-12-15), p. 655-655
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 384, No. 3 ( 2004-12-15), p. 655-655
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/BJ3840655
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 2004
    detail.hit.zdb_id: 1473095-9
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  • 2
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    Primary structure of a Thomsen-Friedenreich-antigen-specific lectin, jacalin [ Artocarpus integrifolia (jack fruit) agglutinin]. Evidence for the presence of an internal repeat
    Portland Press Ltd. ; 1992
    In:  Biochemical Journal Vol. 284, No. 1 ( 1992-05-15), p. 95-101
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 284, No. 1 ( 1992-05-15), p. 95-101
    Abstract: Jacalin [Artocarpus integrifolia (jack fruit) agglutinin] is made up of two types of chains, heavy and light, with M(r) values of 16,200 +/- 1200 and 2090 +/- 300 respectively (on the basis of gel-permeation chromatography under denaturing conditions). Its complete amino acid sequence was determined by manual degradation using a 4-dimethylaminoazobenzene 4′-isothiocyanate double-coupling method. Peptide fragments for sequence analysis were obtained by chemical cleavages of the heavy chain with CNBr, hydroxylamine hydrochloride and iodosobenzoic acid and enzymic cleavage with Staphylococcus aureus proteinase. The peptides were purified by a combination gel-permeation and reverse-phase chromatography. The light chains, being only 20 residues long, could be sequenced without fragmentation. Amino acid analyses and carboxypeptidase-Y-digestion C-terminal analyses of the subunits provided supportive evidence for their sequence. Computer-assisted alignment of the jacalin heavy-chain sequence failed to show sequence similarity to that of any lectin for which the complete sequence is known. Analyses of the sequence showed the presence of an internal repeat spanning residues 7-64 and 76-130. The internal repeat was found to be statistically significant.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2840095
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1992
    detail.hit.zdb_id: 1473095-9
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  • 3
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    Topography of the combining region of a Thomsen-Friedenreich-antigen-specific lectin jacalin ( Artocarpus integrifolia agglutinin). A thermodynamic and circular-dichroism spectroscopic study
    Portland Press Ltd. ; 1990
    In:  Biochemical Journal Vol. 265, No. 3 ( 1990-02-01), p. 831-840
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 265, No. 3 ( 1990-02-01), p. 831-840
    Abstract: 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 explained by considering the thermodynamic parameters in conjunction with the minimum energy conformations of these sugars. It binds to Gal beta 1-3GalNAc alpha Me with 2800-fold stronger affinity over Gal beta 1-3GalNAc beta Me. It does not bind to asialo-GM1 (monosialoganglioside) oligosaccharide. Moreover, it binds to Gal beta 1-3GalNAc alpha Ser, the authentic T (Thomsen-Friedenreich)-antigen, with about 2.5-fold greater affinity as compared with Gal beta 1-3GalNAc. Asialoglycophorin A was found to be about 169,333 times stronger an inhibitor than Gal beta 1-3GalNAc. The present study thus reveals the exquisite specificity of A. integrifolia lectin for the T-antigen. Appreciable binding of disaccharides Glc beta 1-3GalNAc and GlcNAc beta 1-3Gal and the very poor binding of beta-linked disaccharides, which instead of Gal and GalNAc contain other sugars at the reducing end, underscore the important contribution made by Gal and GalNAc at the reducing end for recognition by the lectin. The ligand-structure-dependent alterations of the c.d. spectrum in the tertiary structural region of the protein allows the placement of various sugar units in the combining region of the lectin. These studies suggest that the primary subsite (subsite A) can accommodate only Gal or GalNAc or alpha-linked Gal or GalNAc, whereas the secondary subsite (subsite B) can associate either with GalNAc beta Me or Gal beta Me. Considering these factors a likely arrangement for various disaccharides in the binding site of the lectin is proposed. Its exquisite specificity for the authentic T-antigen, Gal beta 1-3GalNAc alpha Ser, together with its virtual non-binding to A- and B-blood-group antigens, Gal beta 1-3GalNAc beta Me and asialo-GM1 should make A. integrifolia lectin a valuable probe for monitoring the expression of T-antigen on cell surfaces.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2650831
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1990
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  • 4
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    Ribosome-inactivating protein and apoptosis: abrin causes cell death via mitochondrial pathway in Jurkat cells
    Portland Press Ltd. ; 2004
    In:  Biochemical Journal Vol. 377, No. 1 ( 2004-01-01), p. 233-240
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 377, No. 1 ( 2004-01-01), p. 233-240
    Abstract: Abrin belongs to the type II family of ribosome-inactivating proteins comprising a galactose-binding B chain coupled with a toxic A chain through a single disulphide linkage. Apart from its RNA-N-glycosidase activity, another role that has been recently ascribed to abrin was the induction of apoptosis. Studies were undertaken to determine the kinetics of these two activities. In the present study, we report that the signal for apoptosis is triggered at a time point later than the inhibition of protein synthesis. This apoptotic pathway induced by abrin is caspase 3-dependent but caspase 8-independent and involves mitochondrial membrane potential damage and reactive oxygen species production. Overexpression of B-cell lymphocytic-leukaemia proto-oncogene 2 was found to block this apoptotic pathway.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj20030797
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 2004
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  • 5
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    Fluorescence-polarization studies on binding of 4-methylumbelliferyl β- d -galactopyranoside to Ricinus communis (castor-bean) agglutinin
    Portland Press Ltd. ; 1980
    In:  Biochemical Journal Vol. 191, No. 2 ( 1980-11-01), p. 395-400
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 191, No. 2 ( 1980-11-01), p. 395-400
    Abstract: The binding of Ricinus communis (castor-bean) agglutinin 1 to saccharides was studied by equilibrium dialysis and fluorescence polarization by using the fluorescently labelled sugar 4-methylumbelliferyl beta-D-galactopyranoside. No appreciable change in ligand fluorescence of 4-methylumbelliferyl beta-D-galactopyranoside was considerably polarized on its binding to the lectin. The association constants obtained by Scatchard analysis of equilibrium-dialysis and fluorescence-polarization data do not differ much from each other, and at 25 degrees C, Ka = 2.4 (+/- 0.2) X 10(4)M-1. These values agree reasonably well with that reported in the literature for Ricinus agglutinin 1. The number of binding sites obtained by the different experimental procedures is 1.94 +/- 0.1 per molecule of 120 000 daltons and is equal to the reported value of 2. The consistency in the values of Ka and number of binding sites indicate the absence of additional subsites on Ricinus agglutinin 1 for its specific sugars. In addition, the excellent agreement between the binding parameters obtained by equilibrium dialysis and fluorescence polarization indicate the potential of ligand-fluorescence-polarization measurements in the investigation of lectin-sugar interactions.
    Type of Medium: Online Resource
    ISSN: 0264-6021
    URL: Article
    DOI: 10.1042/bj1910395
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1980
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  • 6
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    Studies on tryptophan residues of Abrus agglutinin. Stopped-flow kinetics of modification and fluorescence-quenching studies
    Portland Press Ltd. ; 1987
    In:  Biochemical Journal Vol. 243, No. 1 ( 1987-04-01), p. 79-86
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 243, No. 1 ( 1987-04-01), p. 79-86
    Abstract: The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2430079
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1987
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  • 7
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    Erythrocyte-binding studies on an acidic lectin from winged bean ( Psophocarpus tetragonolobus )
    Portland Press Ltd. ; 1988
    In:  Biochemical Journal Vol. 252, No. 3 ( 1988-06-15), p. 625-631
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 252, No. 3 ( 1988-06-15), p. 625-631
    Abstract: An acidic lectin (WBA II) was isolated to homogeneity from the crude seed extract of the winged bean (Psophocarpus tetragonolobus) by affinity chromatography on lactosylaminoethyl-Bio-Gel. Binding of WBA II to human erythrocytes of type-A, -B and -O blood groups showed the presence of 10(5) receptors/cell, with high association constants (10(6)-10(8) M-1). Competitive binding studies with blood-group-specific lectins reveal that WBA II binds to H- and T-antigenic determinants on human erythrocytes. Affinity-chromatographic studies using A-, B-, H- and T-antigenic determinants coupled to an insoluble matrix confirm the specificity of WBA II towards H- and T-antigenic determinants. Inhibition of the binding of WBA II by various sugars show that N-acetylgalactosamine and T-antigenic disaccharide (Thomsen-Friedenreich antigen, Gal beta 1-3GalNAc) are the most potent mono- and di-saccharide inhibitors respectively. In addition, inhibition of the binding of WBA II to erythrocytes by dog intestine H-fucolipid prove that the lectin binds to H-antigenic determinant.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2520625
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1988
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  • 8
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    Chemical modification studies on Abrus agglutinin. Involvement of tryptophan residues in sugar binding
    Portland Press Ltd. ; 1984
    In:  Biochemical Journal Vol. 217, No. 3 ( 1984-02-01), p. 773-781
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 217, No. 3 ( 1984-02-01), p. 773-781
    Abstract: The galactose-binding lectin from the seeds of the jequirity plant (Abrus precatorius) was subjected to various chemical modifications in order to detect the amino acid residues involved in its binding activity. Modification of lysine, tyrosine, arginine, histidine, glutamic acid and aspartic acid residues did not affect the carbohydrate-binding activity of the agglutinin. However, modification of tryptophan residues carried out in native and denaturing conditions with N-bromosuccinimide and 2-hydroxy-5-nitrobenzyl bromide led to a complete loss of its carbohydrate-binding activity. Under denaturing conditions 30 tryptophan residues/molecule were modified by both reagents, whereas only 16 and 18 residues/molecule were available for modification by N-bromosuccinimide and 2-hydroxy-5-nitrobenzyl bromide respectively under native conditions. The relative loss in haemagglutinating activity after the modification of tryptophan residues indicates that two residues/molecule are required for the carbohydrate-binding activity of the agglutinin. A partial protection was observed in the presence of saturating concentrations of lactose (0.15 M). The decrease in fluorescence intensity of Abrus agglutinin on modification of tryptophan residues is linear in the absence of lactose and shows a biphasic pattern in the presence of lactose, indicating that tryptophan residues go from a similar to a different molecular environment on saccharide binding. The secondary structure of the protein remains practically unchanged upon modification of tryptophan residues, as indicated by c.d. and immunodiffusion studies, confirming that the loss in activity is due to modification only.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2170773
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1984
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  • 9
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    A rapid and sensitive assay for detection of nanogram quantities of castor-bean (Ricinus communis) lectins
    Portland Press Ltd. ; 1979
    In:  Biochemical Journal Vol. 183, No. 1 ( 1979-10-01), p. 185-188
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 183, No. 1 ( 1979-10-01), p. 185-188
    Abstract: Inhibition of lysozyme conjugated with p-aminophenyl beta-D-galactopyranoside by galactose-specific lectins from castor beans (Ricinus communis) has been utilized for assaying these lectins in the nanogram range.
    Type of Medium: Online Resource
    ISSN: 0264-6021
    URL: Article
    DOI: 10.1042/bj1830185
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1979
    detail.hit.zdb_id: 1473095-9
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  • 10
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    Thermodynamic and kinetic studies on saccharide binding to soya-bean agglutinin
    Portland Press Ltd. ; 1986
    In:  Biochemical Journal Vol. 234, No. 3 ( 1986-03-15), p. 515-522
    Details
    In: Biochemical Journal, Portland Press Ltd., Vol. 234, No. 3 ( 1986-03-15), p. 515-522
    Abstract: The fluorescence of N-dansylgalactosamine [N-(5-dimethylaminonaphthalene-1-sulphonyl)galactosamine] was enhanced 11-fold with a 25 nm blue-shift in the emission maximum upon binding to soya-bean agglutinin (SBA). This change was used to determine the association constants and thermodynamic parameters for this interaction. The association constant of 1.51 × 10(6) M-1 at 20 degrees C indicated a very strong binding, which is mainly due to a relatively small entropy value, as revealed by the thermodynamic parameters: delta G = −34.7 kJ × mol-1, delta H = −37.9 kJ × mol-1 and delta S = −10.9 J × mol-1 × K-1. The specific binding of this sugar to SBA shows that the lectin can accommodate a large hydrophobic substituent on the C-2 of ga lactose. Binding of non-fluorescent ligands, studied by monitoring the fluorescence changes when they are added to a mixture of SBA and N-dansylgalactosamine, indicates that a hydrophobic substituent at the anomeric position increases the affinity of the interaction. The C-6 hydroxy group also stabilizes the binding considerably. Kinetics of binding of N-dansylgalactosamine to SBA studied by stopped-flow spectrofluorimetry are consistent with a single-step mechanism and yielded k+1 = 2.4 × 10(5) M-1 × s-1 and k-1 = 0.2 s-1 at 20 degrees C. The activation parameters indicate an enthalpicly controlled association process.
    Type of Medium: Online Resource
    ISSN: 0264-6021 , 1470-8728
    URL: Article
    DOI: 10.1042/bj2340515
    RVK:
    WA 15000
    Language: English
    Publisher: Portland Press Ltd.
    Publication Date: 1986
    detail.hit.zdb_id: 1473095-9
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