Isolation and characterization of a novel serine proteinase complexed with alpha sub(2)-macroglobulin from porcine gastric mucosa

Porcine stomach mucosa was found to contain a 740-kDa protein having endopeptidase activity toward peptide 4-methylcoumaryl-7-amide substrates and low molecular mass peptides. This protein was purified to an apparent homogeneity by a series of chromatographic steps on DEAE-cellulose, Sepharose CL-4B...

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Bibliographic Details
Published in:The Journal of biological chemistry 1993-01, Vol.268 (1), p.527-533
Main Authors: Uchino, T, Sakurai, Y, Nishigai, M, Takahashi, T, Arakawa, H, Ikai, A, Takahashi, K
Format: Article
Language:English
Subjects:
alpha 2-macroglobulin
characterization
complex
isolation
pigs
serine proteinase
stomach
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Summary:Porcine stomach mucosa was found to contain a 740-kDa protein having endopeptidase activity toward peptide 4-methylcoumaryl-7-amide substrates and low molecular mass peptides. This protein was purified to an apparent homogeneity by a series of chromatographic steps on DEAE-cellulose, Sepharose CL-4B, hydroxylapatite, and fast protein liquid chromatography Mono Q columns. Substrate specificity studies using synthetic and peptide substrates indicated that the enzyme preferentially hydrolyzes Arg-X bonds and, to a much lesser extent, Lys-X bonds, and is apparently distinct from thrombin, kallikrein, plasmin, and other trypsin-like proteinases so far reported including tryptase.
ISSN:0021-9258