Human urinary kallikrein - biochemical and physiological aspects.
نویسندگان
چکیده
The h i s t o r y of k a l l i k r e i n begins w i t h the d i s c o v e r y of u r i n a r y k a l l i k r e i n more than f i f t y years ago. The r e n a l o r i g i n of u r i n a r y k a l l i k r e i n , though not f i n a l l y proved, i s l a r g e l y accepted. A p o s s i b l e r o l e of k a l l i k r e i n i n the r e g u l a t i o n of kidney f u n c t i o n and blood pressure has been debated f o r a long time (Pisano and Aus t e r , 1976). However, n e i t h e r the question f o r i t s o r i g i n , nor f o r i t s p h y s i o l o g i c a l r o l e i s f i n a l l y s e t t l e d .
منابع مشابه
Specific identification of tissue kallikrein in exocrine tissues and in cell-free translation products with monoclonal antibodies.
A panel of six mouse monoclonal antibodies (IgG1) has been prepared against purified rat urinary kallikrein (EC 3.4.21.35) and characterized. In radioimmunoassay, the antibody titres of ascitic fluid giving 50% binding to 125I-kallikrein range from 1:2 X 10(3) to 1:1 X 10(6). Antibodies from four of the clones show no cross-reactivity with human urinary kallikrein, rat urinary esterase A or ton...
متن کاملExistence of prokallikrein in the kidney. Its biochemical properties compared to three active glandular kallikreins from the kidney, serum, and urine of the rat.
Prokallikrein in the kidney was partially purified with immunoaffinity and DEAE Sephadex A-50 column chromatographies, and its biochemical properties were studied in comparison to three active glandular kallikreins purified from kidney, serum, and urine of the rat. The properties of the enzyme obtained by trypsin activation of prokallikrein were identical with those of active glandular kallikre...
متن کاملPurification of human urinary prokallikrein. Identification of the site of activation by the metalloproteinase thermolysin.
Human urinary active kallikrein and prokallikrein were separated on DEAE-cellulose and octyl-Sepharose columns and both purified to homogeneity by affinity chromatography, gel filtration and hydrophobic h.p.l.c. Prokallikrein was monitored during purification by trypsin activation followed by determination of both amidase and kininogenase activity. After trypsin activation, purified prokallikre...
متن کاملThe isolation and properties of pig submandibular kallikrein.
The kallikrein from pig submandibular glands was highly purified, with an overall yield of 31%. Affinity chromatography on bovine basic pancreatic trypsin inhibitor linked to Sepharose 4B was an especially effective step in the purification procedure, giving a purification factor of 80. The enzyme is a single-chain molecule, occurring, as does pig urinary kallikrein, as a major B-form of appare...
متن کاملThe effect of cations on the activity of human urinary kallikrein.
We studied the effect of ions on the ability of purified human urinary kallikrein to cleave its natural substrate (kininogen) as well as two synthetic substrates, tosylarginine [3H]methyl ester and Pro-Phe-Arg-[3H]benzylamide. The kininogenase activity of kallikrein is markedly dependent upon the concentration of cations in vitro. Kininogenase activity is very low when measured in a low electro...
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...
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ورودعنوان ژورنال:
- Advances in experimental medicine and biology
دوره 120A شماره
صفحات -
تاریخ انتشار 1979