Purification and properties of a lectin from lonchocarpus capassa (apple-leaf) seed
A lectin has been purified from L. capassa seed by ammonium sulphate fractionation and affinity chromatography on a column of D-galactose-derivatized Sepharose. The lectin is a glycoprotein which contains 3.8% neutral carbohydrates comprised of mannose, N-acetylglucosamine, xylose and fucose. The su...
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| Veröffentlicht in: | Phytochemistry (Oxford) 1986-01, Vol.25 (2), p.323-327 |
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| creator | Joubert, Francois J. Sharon, Nathan Merrifield, E.H. |
| description | A lectin has been purified from
L. capassa seed by ammonium sulphate fractionation and affinity chromatography on a column of D-galactose-derivatized Sepharose. The lectin is a glycoprotein which contains 3.8% neutral carbohydrates comprised of mannose, N-acetylglucosamine, xylose and fucose. The subunit
M, of the lectin is 29 000, it has only alanine as N-terminal amino acid and contains 240 amino acids with a high content of acidic and hydroxy amino acids, single residues of methionine and histidine and the absence ofcystine. The lectin of
L. capassa seed is a metalloprotein in that it contains 0.8 mol Ca
2+ and 0.4 mol Mn
2+ per mol. It agglutinates untreated human A, O and B type erythrocytes and rabbit erythrocytes. N-Acetyl-D-galactosamine was the best inhibitor. D-Galactose and various carbohydrates containing this sugar inhibit the hemagglutinating activity of the lectin. The lectin is also inhibited by D-glucose. The amino-terminal sequence of the lectin from
L. capassa seed shows a significant degree of homology with many lectins from leguminous plants and is related to concanavalin A by a circularly permuted sequence homology. |
| doi_str_mv | 10.1016/S0031-9422(00)85474-6 |
| format | Article |
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L. capassa seed by ammonium sulphate fractionation and affinity chromatography on a column of D-galactose-derivatized Sepharose. The lectin is a glycoprotein which contains 3.8% neutral carbohydrates comprised of mannose, N-acetylglucosamine, xylose and fucose. The subunit
M, of the lectin is 29 000, it has only alanine as N-terminal amino acid and contains 240 amino acids with a high content of acidic and hydroxy amino acids, single residues of methionine and histidine and the absence ofcystine. The lectin of
L. capassa seed is a metalloprotein in that it contains 0.8 mol Ca
2+ and 0.4 mol Mn
2+ per mol. It agglutinates untreated human A, O and B type erythrocytes and rabbit erythrocytes. N-Acetyl-D-galactosamine was the best inhibitor. D-Galactose and various carbohydrates containing this sugar inhibit the hemagglutinating activity of the lectin. The lectin is also inhibited by D-glucose. The amino-terminal sequence of the lectin from
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L. capassa seed by ammonium sulphate fractionation and affinity chromatography on a column of D-galactose-derivatized Sepharose. The lectin is a glycoprotein which contains 3.8% neutral carbohydrates comprised of mannose, N-acetylglucosamine, xylose and fucose. The subunit
M, of the lectin is 29 000, it has only alanine as N-terminal amino acid and contains 240 amino acids with a high content of acidic and hydroxy amino acids, single residues of methionine and histidine and the absence ofcystine. The lectin of
L. capassa seed is a metalloprotein in that it contains 0.8 mol Ca
2+ and 0.4 mol Mn
2+ per mol. It agglutinates untreated human A, O and B type erythrocytes and rabbit erythrocytes. N-Acetyl-D-galactosamine was the best inhibitor. D-Galactose and various carbohydrates containing this sugar inhibit the hemagglutinating activity of the lectin. The lectin is also inhibited by D-glucose. The amino-terminal sequence of the lectin from
L. capassa seed shows a significant degree of homology with many lectins from leguminous plants and is related to concanavalin A by a circularly permuted sequence homology.</description><subject>amino acid sequences</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>apple-leaf tree</subject><subject>Biological and medical sciences</subject><subject>characterization</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>hemagglutinating activity</subject><subject>hemagglutination</subject><subject>lectins</subject><subject>Lonchocarpus</subject><subject>Lonchocarpus capassa</subject><subject>Lonchocarpus capassa, Leguminosae</subject><subject>Proteins</subject><subject>purification</subject><subject>seeds</subject><issn>0031-9422</issn><issn>1873-3700</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><recordid>eNqFkEtr3DAUhUVIIZO0P6FUixKShdsr62F7FULIoxBIYDprcUe-alU8lit5Cv33UTLDbLO6m--ce_gY-yzgmwBhvi8BpKg6VdcXAJetVo2qzBFbiLaRlWwAjtnigJyw05z_AIDWxizY8nmbgg8O5xBHjmPPpxQnSnOgzKPnyAdycxi5T3HDhzi639FhmraZO5wwZ-QXOE0DVQOhv-SZqP_IPngcMn3a3zO2urv9efNQPT7d_7i5fqyc7ORcSa-VqL3qXWc6Qq3XvfJNb9CDqAGbpm1JUefEWpFGj06Ra9AAKRCqJZJn7HzXWyb_3VKe7SZkR8OAI8VttkJ1RmqpCqh3oEsx50TeTilsMP23AuyrQvum0L76sQD2TaE1Jfd1_wCzw8EnHF3Ih3CrW9UIKNiXHeYxWvyVCrJa1iBk2VmKjC7E1Y6gouNfoGSzCzQ66kMqem0fwztTXgAPJY71</recordid><startdate>19860101</startdate><enddate>19860101</enddate><creator>Joubert, Francois J.</creator><creator>Sharon, Nathan</creator><creator>Merrifield, E.H.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>19860101</creationdate><title>Purification and properties of a lectin from lonchocarpus capassa (apple-leaf) seed</title><author>Joubert, Francois J. ; Sharon, Nathan ; Merrifield, E.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-3f5412f4dc969ea55bd4f7d6af0120a7788e4e9c1b4e5afac4ec7a60e40148ee3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>amino acid sequences</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>apple-leaf tree</topic><topic>Biological and medical sciences</topic><topic>characterization</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>hemagglutinating activity</topic><topic>hemagglutination</topic><topic>lectins</topic><topic>Lonchocarpus</topic><topic>Lonchocarpus capassa</topic><topic>Lonchocarpus capassa, Leguminosae</topic><topic>Proteins</topic><topic>purification</topic><topic>seeds</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Joubert, Francois J.</creatorcontrib><creatorcontrib>Sharon, Nathan</creatorcontrib><creatorcontrib>Merrifield, E.H.</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><jtitle>Phytochemistry (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Joubert, Francois J.</au><au>Sharon, Nathan</au><au>Merrifield, E.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and properties of a lectin from lonchocarpus capassa (apple-leaf) seed</atitle><jtitle>Phytochemistry (Oxford)</jtitle><date>1986-01-01</date><risdate>1986</risdate><volume>25</volume><issue>2</issue><spage>323</spage><epage>327</epage><pages>323-327</pages><issn>0031-9422</issn><eissn>1873-3700</eissn><abstract>A lectin has been purified from
L. capassa seed by ammonium sulphate fractionation and affinity chromatography on a column of D-galactose-derivatized Sepharose. The lectin is a glycoprotein which contains 3.8% neutral carbohydrates comprised of mannose, N-acetylglucosamine, xylose and fucose. The subunit
M, of the lectin is 29 000, it has only alanine as N-terminal amino acid and contains 240 amino acids with a high content of acidic and hydroxy amino acids, single residues of methionine and histidine and the absence ofcystine. The lectin of
L. capassa seed is a metalloprotein in that it contains 0.8 mol Ca
2+ and 0.4 mol Mn
2+ per mol. It agglutinates untreated human A, O and B type erythrocytes and rabbit erythrocytes. N-Acetyl-D-galactosamine was the best inhibitor. D-Galactose and various carbohydrates containing this sugar inhibit the hemagglutinating activity of the lectin. The lectin is also inhibited by D-glucose. The amino-terminal sequence of the lectin from
L. capassa seed shows a significant degree of homology with many lectins from leguminous plants and is related to concanavalin A by a circularly permuted sequence homology.</abstract><cop>Amsterdam</cop><pub>Elsevier Ltd</pub><doi>10.1016/S0031-9422(00)85474-6</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Phytochemistry (Oxford), 1986-01, Vol.25 (2), p.323-327 |
| issn | 0031-9422 1873-3700 |
| language | eng |
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| source | Elsevier ScienceDirect Journals Complete |
| subjects | amino acid sequences Analytical, structural and metabolic biochemistry apple-leaf tree Biological and medical sciences characterization Fundamental and applied biological sciences. Psychology Glycoproteins hemagglutinating activity hemagglutination lectins Lonchocarpus Lonchocarpus capassa Lonchocarpus capassa, Leguminosae Proteins purification seeds |
| title | Purification and properties of a lectin from lonchocarpus capassa (apple-leaf) seed |
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