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Bryothamnion seaforthii Lectin Relaxes Vascular Smooth Muscle: Involvement of Endothelium and NO Synthase

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Bryothamnion seaforthii lectin (BSL) induced reversible concentration-related relaxation of endothelized aorta, maximal at 30μg/ml (IC50= 4.8 ± 0.6μg/ml). This effect was inhibited by L-NAME and reversed by mucin, probably via interaction with a specific lectin-binding site on the endothelium activating nitric oxide synthase.

Keywords: Bryothamnion seaforthii; Lectin; agglutinin; nitric oxide synthase; red marine alga

Document Type: Research Article


Publication date: 2010-03-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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