Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.11 (CD10)
 9,792 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Using electrophoresis and ultracentrifugation, a homogeneous proteinase was isolated from protofradine, a protease Act. fradiae 119 preparation. The purification procedure included filtration on DEAE-cellulose, gel filtration through Arcylex P-10, CM-chromatography and desalting on Sephadex G-15. The proteinase under study is an endopeptidase which hydrolyzes low molecular weight synthetic trypsin substrates as well as casein and denaturated collagen. Diisopropylfluorophosphate and soya bean trypsin inhibitor completely inhibit the proteinase activity, whereas pCMB and EDTA have no such effect. The stability maximum is observed at pH of 2.5-3.5, the action maximum at pH 8.7-9.5. The amino acid composition of the enzyme is similar to that of trypsin from Str. griseus. The molecular weights of the proteinase as determined by gel filtration and sedimentation equilibrium method are equal to 25400 and 26500, respectively. The isoelectric point lies at 5.3. The data obtained suggest that the proteinase can be attributed to the family of trypsin proteinases.
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PMID:[Trypsin-like proteinase from Actinomyces fradiae 119]. 675 65

A newly-identified protease from rabbit skeletal muscle, named hydrolase H [Okitani, A. et al. (1980) Agric. Biol. Chem. 44, 1705-1708] has been shown to hydrolyze L-leucine beta-naphthylamide as well as alpha-N-benzoyl-DL-arginine beta-naphthylamide. The enzyme hydrolyzes protamine in the manner of an endopeptidase and hydrolyzes tripeptides and tetrapeptides in the manner of an aminopeptidase. Thus it has been concluded that the enzyme possesses the properties of both endopeptidase and aminopeptidase and that it should be classified as an aminoendopeptidase. Both activities of endopeptidase and aminopeptidase are maximal at pH 7.5-8.0 and enhanced remarkably by thiol compounds. Both activities are stable at pH 7-9 and protected by 2-mercaptoethanol. They are inhibited by monoiodoacetic acid, leupeptin, Zn2+ and Ni2+, but not affected by EDTA, trypsin inhibitor, pepstatin, antipain and phenylmethylsulfonyl fluoride. These results suggest that the enzyme is a thiol protease. The enzyme is composed of three kinds of subunits, the chain Mr of which are 51000, 72000 and 92000.
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PMID:Characterization of hydrolase H, a new muscle protease possessing aminoendopeptidase activity. 701 33

An alkaline proteolytic activity from the smooth muscle of mouse small intestine has been separated and characterised. The activity sedimented after high-speed centrifugation, but was released into the soluble phase after treatment with 2.0 M KCl. The proteinase was found to be sensitive to salt concentration and the activity was maximal between 0.1-0.5 M NaCl/KCl and pH 9.5. This activity was completely inhibited by di-isopropylphosphoro fluoridate suggesting that it is a serine endopeptidase. The proteinase was identified as chymotrypsin-like due to the inhibition observed with the agents chymostatin, lima bean and soya bean trypsin inhibitor. These characteristics of the alkaline proteinase resemble the properties of the mast cell enzyme, chymase. The enzyme activity was measured in 48/80 treated animals and the mutant strain w/wv, which do not contain mast cells. No significant reduction in the enzyme activity was observed.
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PMID:Alkaline proteolytic activity from smooth muscle of mouse small intestine. 704 3

1. We have previously shown that atrial natriuretic peptide causes bronchodilatation and reduces bronchial reactivity when administered intravenously or by inhalation to asthmatic patients. We wished to determine the direct effect of exogenously applied atrial natriuretic peptide on isolated airway and the role of proteases important in atrial natriuretic peptide degradation in other organ systems. 2. The ability of atrial natriuretic peptide (alpha-human atrial natriuretic peptide 28-amino acid) to relax precontracted tissues and to protect against methacholine-induced contraction was studied in human and bovine tissue. The role of neutral endopeptidase-24.11 and other proteases in regulating the effect of atrial natriuretic peptide on bronchial smooth muscle was also examined by studying the influence of phosphoramidon, a protease inhibitor, whose actions include the inhibition of neutral endopeptidase-24.11, and the protease inhibitors leupeptin, aprotinin and soybean trypsin inhibitor on the airway response to atrial natriuretic peptide. 3. In human and bovine tissue atrial natriuretic peptide (10(-6) mol/l) caused a slight relaxation of methacholine-contracted tissue [mean (SEM) percentage inhibition of contraction of 13.2 (3.02)% and 9.41 (2.63)% respectively] and evoked a significant rightward shift of the cumulative concentration-response curve to methacholine [pD2 5.15 (0.23) and 4.85 (0.1) compared with control values of 6.14 (0.1) and 5.85 (0.16), respectively]. 4. Phosphoramidon potentiated atrial natriuretic peptide-induced relaxation of methacholine-induced tone and the ability of atrial natriuretic peptide to protect against methacholine-induced contraction. The combination of leupeptine, aprotinin and soybean trypsin inhibitor did not significantly alter the bronchial response to atrial natriuretic peptide in either human or bovine tissues.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Modulation of the effect of atrial natriuretic peptide in human and bovine bronchi by phosphoramidon. 751 55

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. The protein was shown to be a complex of the plasma proteinase inhibitor alpha 2-macroglobulin and a 25-kDa endopeptidase. The enzyme activity was completely inhibited by diisopropyl fluorophosphate, p-amidinophenylmethanesulfonyl fluoride, leupeptin, antipain, bovine pancreatic trypsin inhibitor, soybean trypsin inhibitor, and ovomucoid, indicating that the entrapped enzyme is a serine proteinase. The proteinase could be released from alpha 2-macroglobulin by mild acid treatment and the released enzyme showed activity toward protein substrates. 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. Thus, the present enzyme is thought to be a novel type of serine proteinase. The proteinase associated with alpha 2-macroglobulin was also found in porcine intestinal mucosa, but not in plasma.
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PMID:Isolation and characterization of a novel serine proteinase complexed with alpha 2-macroglobulin from porcine gastric mucosa. 767 2

The effects of enzyme inhibitors on vasoactive intestinal peptide (VIP)-induced decreases in airway opening pressure (PaO) and VIP-like immunoreactivity (VIP-LI) recovery were studied in isolated tracheal superfused guinea pig lungs. In the absence of inhibitors, VIP 0.38 (95% CI 0.33-0.54) nmol/kg animal, resulted in a 50% decrease in PaO and 33% of a 1 nmol/kg VIP dose was recovered as intact VIP. In the presence of two combinations of enzyme inhibitors, SCH 32615 (S, 10 microM) and aprotinin (A, 500 tyrpsin inhibitor units [TIU]/kg) or S and soybean trypsin inhibitor (T, 500 TIU/kg), VIP caused a significantly greater decrease in PaO and greater quantities of VIP were recovered from lung effluent (both P < 0.001). The addition of captopril, (3 microM), leupeptin (4 microM), or bestatin (1 microM) failed to further increase pulmonary relaxation or recovery of VIP-LI. When given singly, A, T, and S did not augment the effects or recovery of VIP. The efficacy of S (a specific inhibitor of neutral endopeptidase [NEP]) and A and T (serine protease inhibitors) thus implicated NEP and at least one serine protease as primary modulators of VIP activity in the guinea pig lung. We sought to corroborate this finding by characterizing the predominant amino acid sites at which VIP is hydrolized in the lung. When [mono(125I)iodo-Tyr10]VIP was offered to the lung, in the presence and absence of the active inhibitors, cleavage products consistent with activity by NEP and a tryptic enzyme were recovered. These data demonstrate that NEP and a peptidase with an inhibitor profile and cleavage pattern compatible with a tryptic enzyme inactivate VIP in a physiologically competitive manner.
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PMID:Peptidase modulation of vasoactive intestinal peptide pulmonary relaxation in tracheal superfused guinea pig lungs. 767 3

Degradation of 125I-labeled endothelin-1 (125I-ET-1) when incubated 120 min at 37 degrees C with rat lung, kidney and liver plasma membrane extracts was examined using HPLC. Lung and kidney extracts showed degrading enzyme activity, but none was found in liver extract. EDTA almost abolished degradation of 125I-ET-1 in lung and kidney extracts. Phosphoramidon and SCH 39370, both inhibitors of neutral endopeptidase 24.11 (NEP), markedly inhibited degradation of 125I-ET-I in lung extract and clearly less in kidney extract. Soybean trypsin inhibitor (STI) and elastase inhibitor partly inhibited degradation in lungs and in kidney extract. Leupeptin had no inhibitory effect neither in lung nor in kidney extract. Our results suggest: (1) at least two types of enzymes degrade ET-1 in lung and kidney extracts, namely metallo-proteinases and serine proteinases. (2) The ET-1 degrading effect appears to be different in lungs and kidneys, metallo-proteinases being more important in pulmonary than in renal degradation of ET-1.
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PMID:Degradation of endothelin-1 by extracts of rat lung, kidney, and liver. 776 21

Two novel trypsin inhibitors, MCTI-II' and BGIT, were isolated from the seeds of bitter gourd (Momordica charantia) and their amino acids sequenced. MCTI-II' was a squash type trypsin inhibitor and lacked the N-terminal arginine residue of Momordica charantia trypsin inhibitor (MCTI)-II. It consists of 27 amino acid residues and forms a dimeric structure. BGIT had 88% homology with bitter gourd inhibitor against an acidic amino acid-specific endopeptidase (BGIA) consisting of 68 amino acid residues and inhibited not only trypsin but also subtilisin Carlsberg. The amino acid replacements occurred in 8 positions of which that of Gln2 by Arg or of Ala44 by Lys is suggested to be responsible for the trypsin-inhibitory action of BGIT. Inhibitory activity of BGIT for trypsin was greatly decreased by acetylation, while that for subtilisin was slightly increased. From these results and the sequence comparison with eglin-c superfamily inhibitors, the reactive site of BGIT is assumed to be Lys44.
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PMID:Isolation and amino acid sequences of two trypsin inhibitors from the seeds of bitter gourd (Momordica charantia). 776 85

In this paper, data are presented on purification and properties of a new serine endopeptidase (duodenase) isolated from bovine duodenum mucosa. The enzyme has been purified to homogeneity by combinations of ammonium sulphate fractionation, carboxymethyl-cellulose 52 chromatography, and affinity chromatography on Sepharose 4B with Kunitz soybean trypsin inhibitor as a ligand. Some physicochemical properties of this protease have been investigated. The molecular mass of the purified duodenase was determined to be 29 +/- 0.5 kDa by SDS/PAGE and G-2000 SW column chromatography. The enzyme molecule is a single chain and the native enzyme is a monomeric protein. Its isoelectric point was estimated to be 10 +/- 0.2. Duodenase has two forms (I and II) which possess similar properties but differ in their amino acid composition. The new protease is a glycoprotein and contains approximately 3.5% sugars. The enzyme displays trypsin-like and chymotrypsin-like activities and hydrolyzes the amide bonds of substrates having Lys, Arg, Tyr, Phe and Leu residues at the P1 position. Duodenase is most active at pH 7.9-8.2. Duodenase was irreversibly inhibited by diisopropylphosphofluoridate and phenylmethanesulphonyl fluoride, indicative of an active-site serine in this protease. alpha-N-Tosyl-L-lysine chloromethane and alpha-N-tosyl-L-phenylalanine chloromethane, which react with an active His, caused marked inhibition of trypsin-like and chymotrypsin-like activities of duodenase. The enzyme activity was strongly suppressed by trypsin inhibitors from different sources (soybeans, bovine lungs and Lima beans). Chicken egg white ovomucoid had no effect on the duodenase activity. The N-terminal sequence of the native duodenase (24 amino acid residues) shows high similarity with those of human and murine cytotoxic T-lymphocyte granzymes, human leukocyte cathepsin G and rat mast cell chymases. The biological role of duodenase is discussed.
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PMID:Duodenase, a new serine protease of unusual specificity from bovine duodenal mucosa. Purification and properties. 786 48

1. Aqueous extracts of Enterolobium contortisiliquum seeds contain an endopeptidase of M(r) 60,000 with specificity for basic amino acid residues. The enzyme was purified by chromatography on DEAE Sephadex, followed by gel filtration on Sephadex G-75 and affinity chromatography on Zinc-Sepharose. The overall purification was 300-fold and the yield about 46%. 2. The endopeptidase hydrolyzes benzoyl-arginine-p-nitroanilide (Bz-Arg-pNan) and acetyl-phenylalanine-arginine-p-nitroanilide (Ac-Phe-Arg-pNan) with Km 14.4 mM and 0.062 mM, respectively. Succinyl-phenylalanine-p-nitroanilide (Suc-Phe-pNan) and tosyl-arginine methyl ester (TAME) were not hydrolyzed. E. contortisiliquum endopeptidase also cleaves a seed protein of low molecular weight from the same E. contortisiliquum seeds, and converts Met-Lys-bradykinin into bradykinin (Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg). 3. Metals (1.0 mM) such as Cr3+, Fe3+ and Zn2+ ions inactivate the enzyme when Bz-Arg-pNan was the substrate. Enzyme activity is abolished by EDTA but is partially restored by Cu2+, Al3+, Ba2+, Mn2+, Mg2+, Fe2+, Ca2+ and Co2+ ions. The endopeptidase is not inhibited by the previously purified E. contortisiliquum inhibitors of trypsin and cysteine proteinases, or by soybean trypsin inhibitor (Oliva et al. (1987). Brazilian Journal of Medical and Biological Research, 20:767-770).
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PMID:Isolation and partial characterization of an endopeptidase from Enterolobium contortisiliquum seeds. 789 43


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