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The purification, composition and specificity of wheat-germ agglutinin
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| Zeitschriftentitel: | Biochemical Journal |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Biochemical Journal, 131, 1973, 1, S. 155-162 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
|
| Schlagwörter: |
| author_facet |
Allen, A. K. Neuberger, A. Sharon, N. Allen, A. K. Neuberger, A. Sharon, N. |
|---|---|
| author |
Allen, A. K. Neuberger, A. Sharon, N. |
| spellingShingle |
Allen, A. K. Neuberger, A. Sharon, N. Biochemical Journal The purification, composition and specificity of wheat-germ agglutinin Cell Biology Molecular Biology Biochemistry |
| author_sort |
allen, a. k. |
| spelling |
Allen, A. K. Neuberger, A. Sharon, N. 0264-6021 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj1310155 <jats:p>1. The purification of wheat-germ agglutinin from commercial wheat germ is described. By ion-exchange chromatography three active proteins (isolectins) were separated, one of which was examined in detail. 2. The amino acid composition is unusual, as 20% of residues are half-cystine and 21% are glycine. Unlike most lectins and contrary to previous reports, this protein is not a glycoprotein. 3. The efficiency of various saccharides as inhibitors of the agglutination reaction was investigated and from this the specificity of the binding site was inferred. Of monosaccharides, only derivatives of glucose with a 2-acetamido group and a free 3-hydroxyl group are effective inhibitors, and glycosides of either anomeric configuration are bound. Oligosaccharides are much more powerful inhibitors of agglutination than are monosaccharides. 4. It is proposed that the binding site consists of three or four subsites with differing specificities, in a cleft in the molecule resembling that proposed for hen's-egg-white lysozyme.</jats:p> The purification, composition and specificity of wheat-germ agglutinin Biochemical Journal |
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Portland Press Ltd., 1973 |
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Portland Press Ltd., 1973 |
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1973 |
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Portland Press Ltd. |
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Biochemical Journal |
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| title |
The purification, composition and specificity of wheat-germ agglutinin |
| title_unstemmed |
The purification, composition and specificity of wheat-germ agglutinin |
| title_full |
The purification, composition and specificity of wheat-germ agglutinin |
| title_fullStr |
The purification, composition and specificity of wheat-germ agglutinin |
| title_full_unstemmed |
The purification, composition and specificity of wheat-germ agglutinin |
| title_short |
The purification, composition and specificity of wheat-germ agglutinin |
| title_sort |
the purification, composition and specificity of wheat-germ agglutinin |
| topic |
Cell Biology Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1042/bj1310155 |
| publishDate |
1973 |
| physical |
155-162 |
| description |
<jats:p>1. The purification of wheat-germ agglutinin from commercial wheat germ is described. By ion-exchange chromatography three active proteins (isolectins) were separated, one of which was examined in detail. 2. The amino acid composition is unusual, as 20% of residues are half-cystine and 21% are glycine. Unlike most lectins and contrary to previous reports, this protein is not a glycoprotein. 3. The efficiency of various saccharides as inhibitors of the agglutination reaction was investigated and from this the specificity of the binding site was inferred. Of monosaccharides, only derivatives of glucose with a 2-acetamido group and a free 3-hydroxyl group are effective inhibitors, and glycosides of either anomeric configuration are bound. Oligosaccharides are much more powerful inhibitors of agglutination than are monosaccharides. 4. It is proposed that the binding site consists of three or four subsites with differing specificities, in a cleft in the molecule resembling that proposed for hen's-egg-white lysozyme.</jats:p> |
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| author | Allen, A. K., Neuberger, A., Sharon, N. |
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| description | <jats:p>1. The purification of wheat-germ agglutinin from commercial wheat germ is described. By ion-exchange chromatography three active proteins (isolectins) were separated, one of which was examined in detail. 2. The amino acid composition is unusual, as 20% of residues are half-cystine and 21% are glycine. Unlike most lectins and contrary to previous reports, this protein is not a glycoprotein. 3. The efficiency of various saccharides as inhibitors of the agglutination reaction was investigated and from this the specificity of the binding site was inferred. Of monosaccharides, only derivatives of glucose with a 2-acetamido group and a free 3-hydroxyl group are effective inhibitors, and glycosides of either anomeric configuration are bound. Oligosaccharides are much more powerful inhibitors of agglutination than are monosaccharides. 4. It is proposed that the binding site consists of three or four subsites with differing specificities, in a cleft in the molecule resembling that proposed for hen's-egg-white lysozyme.</jats:p> |
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| imprint | Portland Press Ltd., 1973 |
| imprint_str_mv | Portland Press Ltd., 1973 |
| institution | DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275 |
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| physical | 155-162 |
| publishDate | 1973 |
| publishDateSort | 1973 |
| publisher | Portland Press Ltd. |
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| recordtype | ai |
| series | Biochemical Journal |
| source_id | 49 |
| spelling | Allen, A. K. Neuberger, A. Sharon, N. 0264-6021 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj1310155 <jats:p>1. The purification of wheat-germ agglutinin from commercial wheat germ is described. By ion-exchange chromatography three active proteins (isolectins) were separated, one of which was examined in detail. 2. The amino acid composition is unusual, as 20% of residues are half-cystine and 21% are glycine. Unlike most lectins and contrary to previous reports, this protein is not a glycoprotein. 3. The efficiency of various saccharides as inhibitors of the agglutination reaction was investigated and from this the specificity of the binding site was inferred. Of monosaccharides, only derivatives of glucose with a 2-acetamido group and a free 3-hydroxyl group are effective inhibitors, and glycosides of either anomeric configuration are bound. Oligosaccharides are much more powerful inhibitors of agglutination than are monosaccharides. 4. It is proposed that the binding site consists of three or four subsites with differing specificities, in a cleft in the molecule resembling that proposed for hen's-egg-white lysozyme.</jats:p> The purification, composition and specificity of wheat-germ agglutinin Biochemical Journal |
| spellingShingle | Allen, A. K., Neuberger, A., Sharon, N., Biochemical Journal, The purification, composition and specificity of wheat-germ agglutinin, Cell Biology, Molecular Biology, Biochemistry |
| title | The purification, composition and specificity of wheat-germ agglutinin |
| title_full | The purification, composition and specificity of wheat-germ agglutinin |
| title_fullStr | The purification, composition and specificity of wheat-germ agglutinin |
| title_full_unstemmed | The purification, composition and specificity of wheat-germ agglutinin |
| title_short | The purification, composition and specificity of wheat-germ agglutinin |
| title_sort | the purification, composition and specificity of wheat-germ agglutinin |
| title_unstemmed | The purification, composition and specificity of wheat-germ agglutinin |
| topic | Cell Biology, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1042/bj1310155 |