Characterization of a kininogenase from rat vascular tissue resembling tissue kallikrein.
نویسندگان
چکیده
منابع مشابه
Characterization of a kininogenase from rat vascular tissue resembling tissue kallikrein.
A kininogenase resembling glandular kallikrein was partially purified from vascular tissue and characterized. Saline-perfused rat tail arteries and veins were homogenized in 0.25 M sucrose containing 10 mM Tris-HCl (pH 7.4). The homogenate was centrifuged at 105,000 g for 60 minutes, and a vascular kininogenase was purified from the supernatant by chromatofocusing, affinity chromatography on im...
متن کاملPurification and characterization of a kallikrein-like T-kininogenase.
A T-kininogenase has been purified to homogeneity from rat submandibular gland extracts by DEAE-Sepharose chromatography and preparative gel electrophoresis. The purified protein has an apparent Mr of 28,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and splits into heavy and light chains with Mr of 22,000 and 6,000 in the presence of dithiothreitol. It is an acidic glycoprote...
متن کاملCharacterization of mouse tissue kallikrein 5.
Mouse tissue kallikreins (Klks) are members of a large, multigene family consisting of 37 genes, 26 of which can code for functional proteins. Mouse tissue kallikrein 5 (Klk5) has long been thought to be one of these functional genes, but the gene product, mK5, has not been isolated and characterized. In the present study, we prepared active recombinant mK5 using an Escherichia coli expression ...
متن کاملIdentification and characterization of a tissue kallikrein in rat skeletal muscles.
A tissue kallikrein was purified from rat skeletal muscle. Characterization of the enzyme showed that it has alpha-N-tosyl-L-arginine methylesterase activity and releases kinin from purified bovine low-Mr kininogen substrate. The pH optimum (9.0) of its esterase activity and the profile of inhibition by serine-proteinase inhibitors are identical with those of purified RUK (rat urinary kallikrei...
متن کاملIdentification, purification, and localization of tissue kallikrein in rat heart.
A tissue kallikrein has been isolated from rat heart extracts by DEAE-Sepharose and aprotinin-affinity column chromatography. The purified cardiac enzyme has both N-tosyl-L-arginine methyl ester esterolytic and kinin-releasing activities, and displays parallelism with standard curves in a kallikrein radioimmunoassay, indicating it to have immunological identity with tissue kallikrein. The enzym...
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ژورنال
عنوان ژورنال: Circulation Research
سال: 1985
ISSN: 0009-7330,1524-4571
DOI: 10.1161/01.res.56.6.816