Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.4 (deaminase)
 5,113 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A plasminogen/plasmin like substance (AHSAA-1), with affinity to lysine column was separated from DEAE-cellulose adsorbed human seminal plasma. Two forms of acidic arginine amidase with different affinities to LBTI (AHSAA-2) and aprotinin columns (AHSAA-3) were separated from the DEAE-cellulose adsorbed preparation and AHSAA-3 was identified as tissue kallikrein. Two basic arginine amidase preparations having affinity to LBTI (BHSAA-1) and aprotinin column were also separated from the CM-cellulose adsorbed human seminal plasma. Three basic arginine amidases with different molecular mass (BHSAA-2 to 4) were separated by Cellulofine GCL-2000 gel filtration from aprotinin adsorbed material and some of their properties were examined.
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PMID:Detection and separation of some arginine amidases including tissue kallikrein from human seminal plasma. 146 64

A highly sensitive biological assay for tissue kallikrein is described, using human kininogen as substrate; and quantitation, by radioimmunoassay, of generated kinins. Using purified human urinary kallikrein as a reference standard we have correlated the kininogenase activity of kallikrein with amidase activity as measured by cleavage of the synthetic substrate S2266.
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PMID:Biological assay for tissue kallikrein: comparison with the synthetic substrate S2266. 146 67

Activity of tissue and blood plasma kallikreins as well as total content of their inactive precursors were studied in rabbit eye structures and media: iris, ciliary body, cornea, vascular striatum, retina, aqueous humor, tear liquid, lacrimal gland by means of fluorimetric procedure using Z-Phe-Arg-MCA as a substrate. Dissimilar capacity of the trypsin soya bean inhibitor and of aprotinin (basic inhibitor of Kunitz type) to inhibit tissue and blood plasma kallikreins enabled to differentiate the enzymatic activity. Lacrimal gland contained the highest activity of tissue kallikrein which amounted to 70% of total Z-Phe-Arg-MCA-hydrolyzing activity of the homogenate. Total Z-Phe-Arg-MCA-amidase activity and activity of individual kallikreins was distinctly lower in all the eye structures and media studied as compared with that of lacrimal gland. Activity of tissue kallikrein was higher than blood serum kallikrein activity in iris, ciliary body, vascular striatum, retina and conjunctiva. The highest content of prekallikreins was found in conjunctiva, aqueous humor, iris and ciliary body. Tissue and blood plasma kallikrein-kinin systems appear to carry out dissimilar functions in eye tissue structures; they are apparently involved in pathogenesis of some eye diseases.
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PMID:[Activity of tissue and plasma kallikrein and level of their precursors in eye tissue structures and media of healthy rabbits]. 172 76

Basic arginine esterase (amidase) with a specific activity of 3.2 mumol N-alpha-tosyl-L-arginine methyl ester (Tos-Arg-Me) esterolysis per A280 was purified about 230-fold from a CM-cellulose absorbed preparation of human seminal plasma. The purified enzyme was a single band with an apparent molecular weight of 3.4-4.1 x 10(4). The amidolytic activity of this enzyme was suppressed by aprotinin, soybean trypsin inhibitor (SBTI), leupeptin, and antipain, while alpha 1-antitrypsin, ovomucoid trypsin inhibitor (OTI), EDTA, and chymostatin had no or weak effect. This enzyme hydrolyzed synthetic basic amino acid derivatives and N-alpha-tosyl-glycyl-L-prolyl-arginine-p-nitroanilide (Tos-Gly-Pro-Arg-pNA) and N-alpha-tert-butyloxycarbonyl-L-leucyl-L-prolyl-L-arginine-p-nitroanilid e (Boc-Leu-Pro-Arg-pNA) were the best substrates. The enzymatic characteristics of present enzyme were clearly different from tissue kallikrein, acrosin, and seminin in human semen.
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PMID:Basic arginine esterase from human seminal plasma: purification and some properties. 175 84

Glandular kallikrein shows a special selectivity for D-Val-Leu-Arg-4-methoxy-2-naphthylamide in comparison with other potential oligopeptide substrates and it provides a useful histochemical substrate, although the reaction may not always be specific. However, in cat submandibular saliva, a biochemical assay using the closely related D-Val-Leu-Arg-7-amino-4-trifluoromethylcoumarin (AFC) as substrate, which affords more sensitive detection, showed that soya bean trypsin inhibitor causes no inhibition. This indicates that there are unlikely to be contaminating enzymes competing for the substrate in this body fluid. Support for this observation has been gained by the useful new enzyme overlay membrane technique for fluorescent assessment of reactive bands of enzymes after isoelectric focusing, using membranes of cellulose acetate impregnated with D-Val-Leu-Arg-AFC. Comparison of results after isoelectric focusing of purified cat submandibular kallikrein with samples of cat submandibular saliva confirmed that the substrate is monospecific for kallikrein in saliva of the cat. This knowledge has enabled us to start assessing the dynamics of the secretion of kallikrein by the gland. Testing individual drops of saliva has shown that an amazingly rapid mobilization of kallikrein occurs in high concentrations on sympathetic nerve stimulation. The corresponding oligopeptide-based inhibitor D-Val-Leu-Arg-chloromethyl ketone was found to be strongly inhibitory of the amidase reaction by kallikrein but showed a low specificity for kallikrein. Nevertheless, its effects have been tested in vivo by the intravascular route and it caused an increase in the resting salivary vascular resistance whether administered close-arterially or intravenously. Thus, it would seem that a kallikrein-like protease does influence the background tone in the vessels and the source of this enzyme is thought to be mast cells.
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PMID:Use of different derivatives of D-Val-Leu-Arg for studying kallikrein activities in cat submandibular glands and saliva. 241 50

Human pancreatic kallikrein (H. Panc. K.) was purified from human pancreas by serial liquid chromatographies. The final preparation had a specific activity of 9.2 AU/A280 (AU: amidase unit for H-Pro-Phe-Arg-MCA) and its N-terminal sequence coincided with the reported sequence determined from cloned cDNA analysis. In HPLC (gel filtration), one symmetrical peak corresponding to a molecular weight of 48,000 was obtained. In SDS-PAGE without 2-mercaptoethanol, one band corresponding to a molecular weight of 52,000 was obtained. Protease inhibitor specificities of H. Panc. K. were the same as those of human urinary kallikrein (HUK) and hog pancreatic kallikrein (hog Panc. K.), while anti-HUK rabbit antibody inhibited the activities of H. Panc. K. and HUK, but not that of hog Panc. K. From the analysis of affinity for concanavalin A and erythroagglutinating phytohemagglutinin, the carbohydrate parts of H. Panc. K. are relatively rich in bi-(or multi-) antennary complex type sugar chains with bisecting GlcNAc compared with those of human salivary kallikrein and HUK. These findings will be a help to clarify the physiological and pathophysiological roles of H. Panc. K. in the pancreas and pancreatic diseases, especially in acute pancreatitis.
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PMID:[Purification of human pancreatic kallikrein and organ-specificities of human glandular kallikreins]. 260 Nov 18

Human pancreatic kallikrein (H.Panc.K.) was purified from human pancreas by ion exchange chromatography on DEAE-cellulose, affinity chromatographies on p-aminobenzamidine Sepharose 6B and aprotinin aminocellulofine, followed by gel filtration on Sephacryl S-200. The final preparation had a specific activity of 9.2 AU/A280 (AU; amidase unit for H-Pro-Phe-Arg-MCA) and its N-terminal sequence coincided with the reported sequence for H.Panc.K.. In HPLC (gel filtration), one symmetrical peak corresponding to a molecular weight of 48,000 was obtained. In SDS-PAGE without 2-mercaptoethanol (2-ME), one band corresponding to a molecular weight of 52,000 was obtained, but with 2-ME, 2 bands, 52,000 and 30,000, were obtained. Km value for MCA was 4.9 x 10(-2) mM. Proteinase inhibitor specificities of H.Panc.K. were the same as those of human urinary kallikrein (HUK) and hog pancreatic kallikrein (hog Panc.K.), while anti-HUK antibody inhibited the activities of H.Panc.K. and HUK, but not that of hog Panc.K.. From the analysis of affinity for concanavalin A (Con A) and erythroagglutinating phytohemagglutinin (E-PHA), the carbohydrate parts of H.Panc.K. are relatively rich in biantennary complex type sugar chains with bisecting GlcNAc compared with those of human salivary kallikrein (H.Saliv.K.) and HUK.
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PMID:Characterization of human pancreatic kallikrein. 261 57

Tissue kallikrein is an enzyme that forms the vasoactive peptide kallidin from an endogenous substrate L-kininogen. Tissue kallikrein has been identified in joint fluids and in inflammatory infiltrates within synovial membranes. It is suggested that tissue kallikrein and kinins have an important role in synovitis and joint damage. Immunoreactive tissue kallikrein and amidase activity were both measured in the synovial fluid of 24 patients with rheumatoid arthritis (RA) and 12 with osteoarthritis (OA). Active enzyme concentrations were higher in RA than in OA and correlated well with the lysosomal enzymes beta-glucuronidase and lactate dehydrogenase. Both total immunoreactive tissue kallikrein and the proenzyme values were similar in RA and OA. Tissue kallikrein was localised by immunocytochemistry to the polymorphonuclear leucocytes present in the synovial fluid and membranes of patients with RA.
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PMID:A tissue kallikrein in the synovial fluid of patients with rheumatoid arthritis. 264 23

We have identified a tissue kallikrein in polymorphonuclear (PMN) leucocytes of normal human blood and bone marrow by immunocytochemistry, radioimmunoassay and enzymology. Immunoreactive tissue kallikrein was visualized in the mature neutrophil leucocytes and in immature forms such as metamyelocytes and myelocytes. No tissue kallikrein was detected in eosinophil leucocytes, lymphocytes, macrophages, megakaryocytes and platelets. So far, we have failed to observe immunoreactivity to tissue kallikrein in basophils. The presence of tissue kallikrein in extracts prepared from PMN leucocytes isolated from peripheral blood was demonstrated by immunodiffusion, dot-blotting and by radioimmunoassay. The kininogenase and amidase activity of the extracts resembled that of tissue kallikrein in being resistant to soya bean trypsin inhibitor and sensitive to trasylol. The amidase activity attributable to tissue kallikrein was completely inhibited by specific antisera.
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PMID:Identification of a tissue kallikrein in human polymorphonuclear leucocytes. 276

The measurement of glandular kallikrein in biological fluids most often utilizes a synthetic substrate, H-D-valylleucylarginine-p-nitroanilide (S-2266), which assesses amidase activity. Although this substrate has reasonable specificity for glandular kallikrein, other tryptic-like proteases found in mixed saliva may also cause hydrolysis. The primary purpose of this study was to assess the accuracy of the use of this substrate for the measurement of glandular kallikrein in human mixed saliva. An additional objective was to determine the presence of prekallikrein in mixed saliva. The addition of soybean trypsin inhibitor (SBTI), which inhibits other tryptic-like enzymes but not glandular kallikrein, resulted in an approx. 30 per cent decrease in the hydrolysis of S-2266 by centrifuged mixed human saliva. A correlation of 0.918 was obtained between the biological assays for kinin release and amidase activity in 19 subject samples. Amidase activity increased following treatment of saliva with trypsin, indicating the presence of prekallikrein in human mixed saliva. It is concluded that S-2266 is an accurate substrate for the assay of glandular kallikrein in human mixed saliva; that the inclusion of SBTI in the assay mixture is needed to inhibit non-kallikrein proteases that may also hydrolyse the synthetic substrate; and that prekallikrein is present in mixed saliva. Thus any future studies of changes in the level of kallikrein in saliva may wish to consider the presence of both active and total levels of glandular kallikrein.
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PMID:The assay of glandular kallikrein and prekallikrein in human mixed saliva. 324 88


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