Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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

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

We have measured concentrations of tissue kallikrein-like amidase (TKLA) in blood-free rat gastrointestinal tissue. TKLA was present in the gut wall from the stomach to the rectum with concentration peaks in the duodenum and caecum. When rats, fasted for 24 hr were compared with normally fed animals, the mean fasted TKLA levels rose significantly in the duodenum and proximal and distal colons and fell in the caecum. No other tissues showed concentration changes. Sodium chenodeoxycholate and other bile acids have biological actions on the rat intestinal wall which are similar to those produced by the kallikrein-kinin system. We have previously reported that bile acids released TKLA from the rat colon wall. This TKLA was totally inhibited by aprotinin. We now report that intraluminal sodium chenodeoxycholate (30 mM) increases both colonic motility and colonic mucosal leakage. These increases are largely blocked by aprotinin. The ability of intraluminal sodium taurochenodeoxycholate to increase vascular leakage in the rat stomach and colon was parallelled by its ability to release TKLA from these issues. Our results are compatible with the mediation of these biological actions of the tested bile acids via activation of a serine proteinase, possibly tissue kallikrein.
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PMID:Bile acids and the intestinal kallikrein-kinin system. 364 18

A series of acetyl-peptidyl-amides containing the amino acid sequence around the Arg-Ser kallikrein cleavage site of bovine kininogen were synthesized and tested for their ability to inhibit both the kinin-releasing activity and the amidase activity of purified human urinary kallikrein. The substrate analogues were competitive inhibitors for human urinary kallikrein and the heptapeptides (P4-P3'), hexapeptides (P3-P3'), and pentapeptides (P2-P3') gave Ki values of 140, 64, and 18 microM respectively, while the tetrapeptides (P1-P3'), tripeptides (P1'-P3') and dipeptides (P2'-P3') had little or no inhibitory activity. The effective analogues had neither kinin-like nor kinin-blocking activity on the rat uterus either before or after exposure to human urinary kallikrein. The effective human urinary kallikrein inhibitors were further examined for their effect on other serine proteases, including human plasma kallikrein, plasmin, complement components (C1s, C1r), bovine coagulation factors (IIa, IXa, and Xa), elastase, and trypsin. These peptides showed little inhibition of the circulating serine proteases but yielded a Ki for the nonspecific protease trypsin in the microM range. These results should provide the basis for the development of highly specific tissue kallikrein inhibitors to aid in elucidating the in vivo role(s) of tissue kallikreins.
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PMID:Specificity of substrate analogue inhibitors of human urinary kallikrein. 384 67

Human seminal plasma trypsin-like proteinase inhibitor (HSTPI) was separated and examined by trypsin Cellulofine affinity adsorption and Cellulofine GCL-300 gel filtration and its inhibitory action toward some arginine amidases obtained from the urine, semen, and blood of humans. HSTPI showed strong inhibitory action toward two types of human seminal plasma basic arginine amidases (BHSAA-L and -A), human seminal plasma acidic arginine amidase with affinity to lima bean trypsin inhibitor (LBTI) column (AHSAA-L), and human acrosin and thrombin. Conversely, no or little inhibition was observed toward human urinary arginine amidase-2, human high molecular weight urokinase, or human seminal plasma acidic arginine amidase with affinity to aprotinin column (AHSAA-A, tissue kallikrein). Measurement of Ki values of BHSAA-L with affinity to LBTI column toward HSTPI and LBTI revealed that the arginine amidase had a stronger affinity for LBTI than that for HSTPI. This indicates that it is the difference in Ki values that allows BHSAA-L to be separated by the LBTI affinity adsorption method from human seminal plasma containing a large amount of HSTPI.
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PMID:Human seminal plasma proteinase inhibitor: action toward some trypsin-like arginine amidases from humans. 837 82

We studied some of the components of the kininogen-kallikrein-kinin system, simultaneously, in plasma and synovial effusions of patients with inflammatory articular diseases. Plasma and tissue kallikrein like activity and kininogen levels were evaluated. Active plasma and tissue kallikreins in plasma and synovial fluid were detected by their amidase activity upon specific chromogenic substrates. Kininogen levels were determined by a bioassay. Both specific amidase activity of plasma and tissue kallikreins were augmented in synovial effusions in relation to their own plasma activity. Kininogen levels in synovial fluid tended to be diminished in relation to plasma, however statistical significance was not reached. The consumption of kininogen is probably related to kinin production. This finding together with increased activities of plasma and tissue kallikreins reinforce the involvement of kinins in pathogenesis of inflammatory articular diseases.
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PMID:Augmented plasma and tissue kallikrein like activity in synovial fluid of patients with inflammatory articular diseases. 874 Oct 10


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