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Score: 13.00 |
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| Title: Purification of human erythrocytes specific lectins from rice bean , Phaseolus calcaratus syn .
Vigna umbellata , by high-performance liquid chromatography .
| | Author: Datta PK Basu PS Datta TK .
| | Journal: J Chromatogr .
Citation: V : 431 ( 1 ) P : 37-44 Year: 1988 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub3235536 Accession (PMID): 3235536 | | Abstract: Two lectins , an N-acetylgalactosamine-binding lectin , lectin-I , which reacts specifically with human erythrocytes of blood group A , and a galactose-binding lectin , lectin-II , which is specific for human blood group B erythrocytes , have been isolated and purified from rice bean , Phaseolus calcaratus syn .
Vigna umbellata , by a salt solubility pH-dependent method , chromatofocusing and high-performance liquid chromatography .
The homogeneity of the lectins was determined by liquid chromatography and polyacrylamide gel electrophoresis .
The purified lectin-I of molecular mass 80 , 000 is possibly composed of two subunits of molecular mass ca 18 , 000 and 22 , 000 , respectively , whereas lectin-II of molecular mass 100 , 000 appears to be composed of a monomeric protein of molecular mass 25 , 000 .
One endogenous lectin-binding protein was also isolated and purified by liquid chromatography .
The endogenous lectin-binding protein of molecular mass 40 , 000 affects the activity of the A-group specific lectin more than that of the B-group specific lectin .
The endogenous lectin-binding protein appears to be composed of a monomeric protein of molecular mass 20 , 000 .
| Matching Sentences:
[ Sen. 1, subscore: 5.00 ]: Two lectins , an N-acetylgalactosamine-binding lectin , lectin-I , which reacts specifically with human erythrocytes of blood group A , and a galactose-binding lectin , lectin-II , which is specific for human blood group B erythrocytes , have been isolated and purified from rice bean , Phaseolus calcaratus syn .
[ Sen. 6, subscore: 3.00 ]: The endogenous lectin-binding protein of molecular mass 40 , 000 affects the activity of the A-group specific lectin more than that of the B-group specific lectin .
[ Sen. 4, subscore: 2.00 ]: The purified lectin-I of molecular mass 80 , 000 is possibly composed of two subunits of molecular mass ca 18 , 000 and 22 , 000 , respectively , whereas lectin-II of molecular mass 100 , 000 appears to be composed of a monomeric protein of molecular mass 25 , 000 .
[ Sen. 3, subscore: 1.00 ]: The homogeneity of the lectins was determined by liquid chromatography and polyacrylamide gel electrophoresis .
[ Sen. 5, subscore: 1.00 ]: One endogenous lectin-binding protein was also isolated and purified by liquid chromatography .
[ Sen. 7, subscore: 1.00 ]: The endogenous lectin-binding protein appears to be composed of a monomeric protein of molecular mass 20 , 000 .
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Score: 12.00 |
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| Title: Isolation , molecular and biological properties of a lectin from rice embryo : relationship with wheat germ agglutinin properties .
| | Author: Tabary F Font J Bourrillon R | | Journal: Arch . Biochem . Biophys . Citation: V : 259 ( 1 ) P : 79-88 Year: 1987 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub3688888 Accession (PMID): 3688888 | | Abstract: Rice lectin ( Oryza sativa , var .
Balilla 28 ) was purified from defatted embryos by aqueous acid extraction at pH 1 . 3 followed by ammonium sulfate precipitation between 2 and 4 M , affinity chromatography on agarose-p-aminophenyl-beta-D-N-acetylglucosamine , and gel filtration on AcA 54 .
The homogeneity of the lectin was checked by polyacrylamide gel electrophoresis , gel filtration , and immunodiffusion .
The amino acid analysis revealed a high half-cystine content ( 9% ) and a low aromatic and hydrophobic amino acid content .
The lectin contained neither neutral carbohydrates nor amino sugars .
The isoelectric point was estimated to be 8 . 1 .
The molecular weight of rice lectin was estimated to be 38 , 000 .
Sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions showed two polypeptides with Mr 19 , 000 and 15 , 000 .
The circular dichroism spectrum of rice lectin in far ultraviolet was characterized by a positive maximum at 228 nm and a negative band at 203 nm suggesting the presence of a beta-pleated sheet and the absence of alpha-helix .
Rice lectin had no human blood group specificity and agglutinated rabbit erythrocytes more efficiently than erythrocytes from other animal species .
Furthermore , agglutination was enhanced by trypsin treatment of erythrocytes .
The erythroagglutinating activity was very high since the minimal concentration needed to agglutinate erythrocytes was 0 . 05 micrograms/ml .
Although [ methyl-3H ] thymidine incorporation was stimulated in human lymphocytes , rice lectin could not be considered as a mitogenic lectin since it stimulated neither blast transformation nor lymphocyte proliferation .
The saccharide specificity of rice lectin was related to N-acetylglucosamine and its oligomers : N , N , N"-triacetylchitotriose was the most powerful inhibitor .
Furthermore , the N-acetylneuraminic acid was not a specific rice determinant .
Finally , the double immunodiffusion method revealed a cross-reactivity between rice lectin and wheat germ agglutinin , indicating that these lectins were closely antigenically related .
The analogies and differences between biological and immunological properties of rice lectin and wheat germ agglutinin are discussed and the possibility of their evolution from a common ancestor is put forward . | Matching Sentences:
[ Sen. 13, subscore: 2.00 ]: Although [ methyl-3H ] thymidine incorporation was stimulated in human lymphocytes , rice lectin could not be considered as a mitogenic lectin since it stimulated neither blast transformation nor lymphocyte proliferation .
[ Sen. 16, subscore: 2.00 ]: Finally , the double immunodiffusion method revealed a cross-reactivity between rice lectin and wheat germ agglutinin , indicating that these lectins were closely antigenically related .
[ Sen. 1, subscore: 1.00 ]: Rice lectin ( Oryza sativa , var .
[ Sen. 3, subscore: 1.00 ]: The homogeneity of the lectin was checked by polyacrylamide gel electrophoresis , gel filtration , and immunodiffusion .
[ Sen. 5, subscore: 1.00 ]: The lectin contained neither neutral carbohydrates nor amino sugars .
[ Sen. 7, subscore: 1.00 ]: The molecular weight of rice lectin was estimated to be 38 , 000 .
[ Sen. 9, subscore: 1.00 ]: The circular dichroism spectrum of rice lectin in far ultraviolet was characterized by a positive maximum at 228 nm and a negative band at 203 nm suggesting the presence of a beta-pleated sheet and the absence of alpha-helix .
[ Sen. 10, subscore: 1.00 ]: Rice lectin had no human blood group specificity and agglutinated rabbit erythrocytes more efficiently than erythrocytes from other animal species .
[ Sen. 14, subscore: 1.00 ]: The saccharide specificity of rice lectin was related to N-acetylglucosamine and its oligomers : N , N , N"-triacetylchitotriose was the most powerful inhibitor .
[ Sen. 17, subscore: 1.00 ]: The analogies and differences between biological and immunological properties of rice lectin and wheat germ agglutinin are discussed and the possibility of their evolution from a common ancestor is put forward .
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Score: 11.00 |
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| Title: Subcellular site of lectin synthesis in developing rice embryos .
| | Author: Stinissen HM Peumans WJ Chrispeels MJ .
| | Journal: Citation: V : 3 ( 9 ) P : 1979-1985 Year: 1984 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub16453545 Accession (PMID): 16453545 | | Abstract: Embryos of developing rice ( Oryza sativa L cv .
Koshihikari ) caryopses which actively synthesize lectin were labelled with [ S ] cysteine for different times and newly synthesized rice lectin was isolated by affinity chromatography .
Gel filtration of embryo extracts on Sepharose-4B indicated that a large portion of the labelled lectin was associated with the particulate fraction .
Experiments with detergent indicated that this lectin was sequestered within organelles .
When extracts of pulse-labelled embryos were fractionated on isopycnic sucrose gradients , this detergent-released lectin banded in the same density-region as the endoplasmic reticulum ( ER ) marker enzyme NADH-cytochrome c reductase .
Both radioactivity in rice lectin and the enzyme activity shifted towards a higher density in the presence of 2 mM Mg acetate , indicating that the labelled lectin was associated with the rough ER .
The ER-bound lectin could be chased from this organelle when it issue was incubated in unlabelled cysteine following a 1 h pulse of labelled cysteine .
Radioactivity chased out of the ER with a half-life of 4 h and accumulated in the soluble fraction .
In the ER the lectin was present as a polypeptide with mol . wt .
23 000 , while in the soluble fraction it occurred as polypeptides with mol . wt .
18 000 , 10 000 and 8000 .
The rice lectin in the ER is capable of binding carbohydrates since it binds readily to the affinity gels .
It is associated into dimers with an approximate mol . wt . of 46 000 .
The results show that newly synthesized rice lectin is transiently sequestered within the ER before further transport and processing take place . | Matching Sentences:
[ Sen. 2, subscore: 2.00 ]: Koshihikari ) caryopses which actively synthesize lectin were labelled with [ S ] cysteine for different times and newly synthesized rice lectin was isolated by affinity chromatography .
[ Sen. 6, subscore: 2.00 ]: Both radioactivity in rice lectin and the enzyme activity shifted towards a higher density in the presence of 2 mM Mg acetate , indicating that the labelled lectin was associated with the rough ER .
[ Sen. 3, subscore: 1.00 ]: Gel filtration of embryo extracts on Sepharose-4B indicated that a large portion of the labelled lectin was associated with the particulate fraction .
[ Sen. 4, subscore: 1.00 ]: Experiments with detergent indicated that this lectin was sequestered within organelles .
[ Sen. 5, subscore: 1.00 ]: When extracts of pulse-labelled embryos were fractionated on isopycnic sucrose gradients , this detergent-released lectin banded in the same density-region as the endoplasmic reticulum ( ER ) marker enzyme NADH-cytochrome c reductase .
[ Sen. 7, subscore: 1.00 ]: The ER-bound lectin could be chased from this organelle when it issue was incubated in unlabelled cysteine following a 1 h pulse of labelled cysteine .
[ Sen. 9, subscore: 1.00 ]: In the ER the lectin was present as a polypeptide with mol . wt .
[ Sen. 12, subscore: 1.00 ]: The rice lectin in the ER is capable of binding carbohydrates since it binds readily to the affinity gels .
[ Sen. 14, subscore: 1.00 ]: The results show that newly synthesized rice lectin is transiently sequestered within the ER before further transport and processing take place .
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Score: 11.00 |
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| Title: Possible mechanism for the inhibition of lectin-erythrocyte interaction in presence of endogenous lectin receptor .
| | Author: Basu PS Datta PK Datta TK .
| | Journal: Biosci . Rep . Citation: V : 16 ( 6 ) P : 453-8 Year: 1996 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub9062696 Accession (PMID): 9062696 | | Abstract: The presence of hydrophobic sites in the lectin-I molecule was indicated by hydrophobic probes like 1-anilinonapthalene-8-sulfonic acid ( ANS ) , 2-p-toluidinyl napthalene-6-sulfonic acid ( TNS ) .
N-phenyl-1-napthylamine ( NA ) and rose bengal ( RB ) .
This was further confirmed by amino acid modifications in the hydrophobic region of the lectin-I molecule .
The binding of ANS , TNS , NA and RB to lectin-I was affected in the presence of NaCl .
The involvement of hydrophobic interactions in rice-bean lectin-I-endogenous lectin receptor ( ELR ) complex were indicated by alterations in the circular dichroism and fluorescence emission spectra .
The percentage of beta-conformation ( 55-63% ) of lectin-I was decreased by addition of ELR .
ELR on reacting with lectin-I reduced the fluorescence emissions of the hydrophobic probes while fluorescence emission of ANS , TNS , NA and RB were greatly enhanced in presence of lectin-I alone .
N-aceyl-galactosamine did not change the fluorescence emissions of any of the hydrophobic probes in presence or in absence of lectin-I This demonstrates that carbohydrate and hydrophobic sites may be different and non-interacting .
It is proposed that the ELR in reacting with lectin-I , induced conformational changes in the lectin-I molecule and thereby affected its erythroagglutinating activity with human blood group "A" erythrocytes .
| Matching Sentences:
[ Sen. 5, subscore: 2.00 ]: The involvement of hydrophobic interactions in rice-bean lectin-I-endogenous lectin receptor ( ELR ) complex were indicated by alterations in the circular dichroism and fluorescence emission spectra .
[ Sen. 7, subscore: 2.00 ]: ELR on reacting with lectin-I reduced the fluorescence emissions of the hydrophobic probes while fluorescence emission of ANS , TNS , NA and RB were greatly enhanced in presence of lectin-I alone .
[ Sen. 9, subscore: 2.00 ]: It is proposed that the ELR in reacting with lectin-I , induced conformational changes in the lectin-I molecule and thereby affected its erythroagglutinating activity with human blood group "A" erythrocytes .
[ Sen. 1, subscore: 1.00 ]: The presence of hydrophobic sites in the lectin-I molecule was indicated by hydrophobic probes like 1-anilinonapthalene-8-sulfonic acid ( ANS ) , 2-p-toluidinyl napthalene-6-sulfonic acid ( TNS ) .
[ Sen. 3, subscore: 1.00 ]: This was further confirmed by amino acid modifications in the hydrophobic region of the lectin-I molecule .
[ Sen. 4, subscore: 1.00 ]: The binding of ANS , TNS , NA and RB to lectin-I was affected in the presence of NaCl .
[ Sen. 6, subscore: 1.00 ]: The percentage of beta-conformation ( 55-63% ) of lectin-I was decreased by addition of ELR .
[ Sen. 8, subscore: 1.00 ]: N-aceyl-galactosamine did not change the fluorescence emissions of any of the hydrophobic probes in presence or in absence of lectin-I This demonstrates that carbohydrate and hydrophobic sites may be different and non-interacting .
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Score: 10.00 |
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| Title: Mannose-binding plant lectins : different structural scaffolds for a common sugar-recognition process .
| | Author: Barre A Bourne Y Van Damme EJ Peumans WJ RougEP .
| | Journal: Biochimie Citation: V : 83 ( 7 ) P : 645-51 Year: 2001 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub11522393 Accession (PMID): 11522393 | | Abstract: Mannose-specific lectins are widely distributed in higher plants and are believed to play a role in recognition of high-mannose type glycans of foreign micro-organisms or plant predators .
Structural studies have demonstrated that the mannose-binding specificity of lectins is mediated by distinct structural scaffolds .
The mannose/glucose-specific legume ( eg , Con A , pea lectin ) exhibit the canonical twelve-stranded beta-sandwich structure .
In contrast to legume lectins that interact with both mannose and glucose , the monocot mannose-binding lectins ( eg , the Galanthus nivalis agglutinin or GNA from bulbs ) react exclusively with mannose and mannose-containing N-glycans .
These lectins possess a beta-prism structure .
More recently , an increasing number of mannose-specific lectins structurally related to jacalin ( eg , the lectins from the Jerusalem artichoke , banana or rice ) , which also exhibit a beta-prism organization , were characterized .
Jacalin itself was re-defined as a polyspecific lectin which , in addition to galactose , also interacts with mannose and mannose-containing glycans .
Finally the B-chain of the type II RIP of iris , which has the same beta-prism structure as all other members of the ricin-B family , interacts specifically with mannose and galactose .
This structural diversity associated with the specific recognition of high-mannose type glycans highlights the importance of mannose-specific lectins as recognition molecules in higher plants .
| Matching Sentences:
[ Sen. 4, subscore: 2.00 ]: In contrast to legume lectins that interact with both mannose and glucose , the monocot mannose-binding lectins ( eg , the Galanthus nivalis agglutinin or GNA from bulbs ) react exclusively with mannose and mannose-containing N-glycans .
[ Sen. 6, subscore: 2.00 ]: More recently , an increasing number of mannose-specific lectins structurally related to jacalin ( eg , the lectins from the Jerusalem artichoke , banana or rice ) , which also exhibit a beta-prism organization , were characterized .
[ Sen. 1, subscore: 1.00 ]: Mannose-specific lectins are widely distributed in higher plants and are believed to play a role in recognition of high-mannose type glycans of foreign micro-organisms or plant predators .
[ Sen. 2, subscore: 1.00 ]: Structural studies have demonstrated that the mannose-binding specificity of lectins is mediated by distinct structural scaffolds .
[ Sen. 3, subscore: 1.00 ]: The mannose/glucose-specific legume ( eg , Con A , pea lectin ) exhibit the canonical twelve-stranded beta-sandwich structure .
[ Sen. 5, subscore: 1.00 ]: These lectins possess a beta-prism structure .
[ Sen. 7, subscore: 1.00 ]: Jacalin itself was re-defined as a polyspecific lectin which , in addition to galactose , also interacts with mannose and mannose-containing glycans .
[ Sen. 9, subscore: 1.00 ]: This structural diversity associated with the specific recognition of high-mannose type glycans highlights the importance of mannose-specific lectins as recognition molecules in higher plants .
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