Isolation and characterization of a zinc-containing metalloprotease expressed by Vibrio tubiashii
作者： R B Delston , M H Kothary , K A Shangraw , B D Tall
DOI: 10.1139/W03-067
关键词: Peptide sequence 、 Biochemistry 、 Vibrio 、 Ammonium sulfate precipitation 、 Protease 、 Molecular mass 、 Vibrio tubiashii 、 Vibrionaceae 、 Isoelectric point 、 Biology
摘要: 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, human erythrocytes. has molecular mass of 35 kDa, isoelectric points 3.5 3.7, is inhibited ortho-phenanthro line, phosphoramidon, 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) strong homology to other proteases.Key words: tubiashii, metalloprotease, hemagglutinin.
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