Abstract
A Vibrio tubiashii hemagglutinin, a protease, was purified by ammonium sulfate precipitation, gel filtration, and hydrophobic interaction chromatography. It agglutinates sheep, chicken, bovine, rabbit, guinea pig, and human erythrocytes. It has a molecular mass of 35 kDa, isoelectric points of 3.5 and 3.7, and is inhibited by ortho-phenanthro line, phosphoramidon, and Zincov. The N-terminal amino acid sequence (Ala-Gln-Ala-Thr-Gly-Thr-Gly- Pro-Gly-Gly-Asn-Gln-Lys-Thr-Gly-Gln- Tyr-Asn-Phe-Gly) has strong homology to other Vibrio proteases.
MeSH terms
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Amino Acid Sequence
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Ammonium Sulfate
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Animals
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Chemical Fractionation / methods
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Chromatography / methods
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Glycopeptides / pharmacology
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Hemagglutination
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Humans
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Hydroxamic Acids / pharmacology
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Isoelectric Point
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Metalloproteases / chemistry
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Metalloproteases / genetics
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Metalloproteases / isolation & purification*
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Metalloproteases / metabolism*
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Molecular Sequence Data
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Molecular Weight
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Phenanthrolines / pharmacology
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Protease Inhibitors / pharmacology
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Sequence Homology, Amino Acid
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Vibrio / enzymology*
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Vibrio / genetics
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Zinc / analysis
Substances
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Glycopeptides
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Hydroxamic Acids
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Phenanthrolines
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Protease Inhibitors
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zincov
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Metalloproteases
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Zinc
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Ammonium Sulfate
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phosphoramidon