Isolation and characterization of a flocculating protein from Moringa oleifera Lam
A flocculating protein from the seeds of Moringa oleifera Lam. was isolated by extraction with phosphate buffer followed by cation exchange chromatography. The molecular mass of the protein determined by SDS-PAGE was about 6.5 kDa, the isoelectric point was above pH 10. Amino acid analysis and seque...
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| Hauptverfasser: | , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
13 April 1995
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| In: |
Biochimica et biophysica acta. General subjects
Year: 1995, Jahrgang: 1243, Heft: 3, Pages: 477-481 |
| ISSN: | 1872-8006 |
| DOI: | 10.1016/0304-4165(94)00176-X |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/0304-4165(94)00176-X Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/030441659400176X 
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| Verfasserangaben: | Ursula Gassenschmidt, Klaus D. Jany, Bernhard Tauscher, Heinz Niebergall |
MARC
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| 520 | |a A flocculating protein from the seeds of Moringa oleifera Lam. was isolated by extraction with phosphate buffer followed by cation exchange chromatography. The molecular mass of the protein determined by SDS-PAGE was about 6.5 kDa, the isoelectric point was above pH 10. Amino acid analysis and sequencing showed high contents of glutamine, arginine and proline, and a total of 60 residues. The amino terminus is blocked by pyroglutamate. The flocculant capacity, determined in glass powder suspension, is comparable to that of a cationic polymer on polyacrylamide basis. Flocculation activity may be explained by the patch charge mechanism due to low molecular weight and high charge density. | ||
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| 650 | 4 | |a Flocculating proteins | |
| 650 | 4 | |a Flocculation activity | |
| 650 | 4 | |a Protein sequence | |
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