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  Structural characterization of coagulant Moringa oleifera Lectin and its effect on hemostatic parameters

Luz, L. d. A., Cabral Silva, M. C., Ferreira, R. d. S., Santana, L. A., Silva-Luccao, R. A., Mentele, R., et al. (2013). Structural characterization of coagulant Moringa oleifera Lectin and its effect on hemostatic parameters. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 58, 31-36. doi:10.1016/j.ijbiomac.2013.03.044.

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Luz, Luciana de Andrade1, Autor
Cabral Silva, Mariana Cristina1, Autor
Ferreira, Rodrigo da Silva1, Autor
Santana, Lucimeire Aparecida1, Autor
Silva-Luccao, Rosemeire Aparecida1, Autor
Mentele, Reinhard2, Autor           
Vilela Oliva, Maria Luiza1, Autor
Guedes Paiva, Patricia Maria1, Autor
Breitenbach Barroso Coelho, Luana Cassandra1, Autor
Affiliations:
1external, ou_persistent22              
2Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565158              

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Schlagwörter: CIRCULAR-DICHROISM SPECTRA; SECONDARY STRUCTURE; WATER-TREATMENT; SEEDS; PROTEIN; PURIFICATION; ANTIFUNGAL; ASSAY; OIL; LAMCoagulant Moringa oleifera lectin; Primary sequence; Circular dichroism; Anticoagulant lectin and Hemostatic parameters;
 Zusammenfassung: Lectins are carbohydrate recognition proteins. cMoL, a coagulant Moringa oleifera Lectin, was isolated from seeds of the plant. Structural studies revealed a heat-stable and pH resistant protein with 101 amino acids, 11.67 theoretical pI and 81% similarity with a M. oleifera flocculent protein. Secondary structure content was estimated as 46% alpha-helix, 12% beta-sheets, 17% beta-turns and 25% unordered structures belonging to the alpha/beta tertiary structure class. cMoL significantly prolonged the time required for blood coagulation, activated partial thromboplastin (aPTF) and prothrombin times (PT), but was not so effective in prolonging aPTT in asialofetuin presence. cMoL acted as an anticoagulant protein on in vitro blood coagulation parameters and at least on aPTT, the lectin interacted through the carbohydrate recognition domain. (C) 2013 Elsevier B.V. All rights reserved.

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Sprache(n): eng - English
 Datum: 2013-07
 Publikationsstatus: Erschienen
 Seiten: 6
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000320746200006
DOI: 10.1016/j.ijbiomac.2013.03.044
 Art des Abschluß: -

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Titel: INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS : ELSEVIER SCIENCE BV
Seiten: - Band / Heft: 58 Artikelnummer: - Start- / Endseite: 31 - 36 Identifikator: ISSN: 0141-8130