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

---

Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Total esterase activity of blood plasma from healthy persons was equal to 27.4 +/- 4.96 micrometer/ml/hr, activity of kallikrein--74.4 +/- 8.65 micrometer of hydrolysed substrate/hr/ml of blood plasma, inhibitory capacity of blood plasma towards kallikrein was 0.9 +/- 0.1 app. un. Total esterase activity of blood plasma, reflecting the activity of trypsin-like enzymes and kallikrein, was distinctly increased in patients with hemorrhagic vasculitis as compared with control group; content of prekallikrein and the inhibitory capacity of blood plasma towards kallikrein were decreased. In patients with severe forms of hemorrhagic vasculitis the most pronounced activation of blood kinine system was observed due to decrease in content of kallikrein and in the inhibitory capacity of blood plasma towards kallikrein.
...
PMID:[Role of the blood kinin system in the pathogenesis of the hemorrhagic syndrome in hemorrhagic vasculitis]. 73 77

Contamination of werum by certain gram-negative bacteria has been shown to spoil the serum for measurement of trypsin inhibitory capacity (STIC) or for antitrypsin phenotyping. Such sera develop intense fibrinolytic activity when the STIC has dropped to itsminimal level, but antitrypsin concentration as measured by radial immunodiffusion remainsconstant. Cultures of ENTEROBACTER, Klebsiella, Bacillus subtilis, and Pseudomonas species were shown to have this capability, but production of the fibrinolytic enzyme by the bacteria was most proficient in the presence of human serum. The enzyme is believed to be of bacterial origin because of its lack of esterase activity, and because activation of serum plasmin by streptokinase did not affect the STIC. Care mustbe taken to avoid bacterial contamination of blood that is to be submitted for an STICassay and/or antitrypsin phenotyping. Serum should be prepared quickly, frozen soon,and stored and transported in a frozen state.
...
PMID:Interference with alpha-antitrypsin studues in stored serum by presumed bacterial proteases. 80 60

Procedures were developed for isolating highly purified cytoplasmic granules of basophilic leukocytes from guinea pig peripheral blood. The methods involved disruption of cells in 0.34 M sucrose followed by a series of membrane filtrations and fractionation on sucrose density gradients. These preparations, up to 95% pure basophil granules by electron microscopy, contained a mixture of neutral esterases-proteases including caseinolytic activity; both trypsin- and chymotrypsin-like serine hydrolases were identified by means of appropriate inhibitors. Localization of at least one such activity to the basophil granule was confirmed by a cytochemical method; this activity was absent in contaminating lymphocytes and eosinophils. By contrast, several lysosomal enzymes, lactic dehydrogenase, and plasminogen activator activity, present in cell homogenates, were absent from purified granules. The granule matrix of guinea pig basophils, unlike the cytoplasmic granules of other granulocytes or mast cells, was little altered by high or low salt concentration but was disrupted into insoluble fragments by 0.01 N HCl and by Triton X-100. Granules were solubilized by papain and by urea-SDS but enzyme activity was destroyed. Triton X-100 incubation with freeze-thawing proved to be the optimal method for extracting esterase activities. Esterase activities were not released from basophils under conditions of anaphylactic degranulation that liberated the great majority of basophil granule histamine.
...
PMID:Isolation of the cytoplasmic granules of guinea pig basophilic leukocytes: identification of esterase and protease activities. 87 25

In 153 probands the following parameters of normal parotid gland secretion were examined: flow-rate, total protein excretion, lysozyme, amylase, phosphatase, BAEE-esterase, immunglobulin A and trypsin-inhibitor. The results were compared with secretions of parotid glands with tumors (51 patients), sialadenitis (22 patients) and sialadenosis (12 patients). Thereby differential diagnosis in sialotumors was found possible. The mose important parameters are flow-rate, protein and immunglobulin A-concentrations, Moreover it is possible to differentiate in sialadenitis and sialadenosis: lysocym secretion gives besides flow--rate protein and immunglobulin A-concentration a good parameter in differentiating both pathological findings. Discelectrophoretic and immunoelectrophoretic separations supplement the differential diagnosis in sialotumors, sialadenitis and sialadenosis. The results are discussed.
...
PMID:[Protein composition of human saliva under rest and stimulation and its changes in salivary gland diseases]. 88 Nov 49

Isolation of tropoelastin is complicated by the presence of a neutral protease closely associated with tropoelastin that is capable of sequentially degrading tropoelastin to small peptides. Substrate and inhibitor specificities of this neutral protease associated with purified tropoelastin were examined. The enzyme displayed proteolytic activity against casein, and esterase activity was detected when assayed against N-tosyl-L-arginine methyl ester but not against tert-butyl-oxycarbonyl-L-alanine p-nitrophenyl ester. No appreciable elastinolytic activity was detectable against either insoluble sodium dodecyl sulfate treated elastin or maleylated tropoelastin. The enzyme was not inhibited by the chymotrypsin inhibitor toluenesulfonylphenylalanine chloromethyl ketone. The enzyme was inhibited by phenylmethanesulfonyl fluoride and, to various degrees, by metal chelators. Tosyllysyl chloromethyl ketone, epsilon-aminocaproic acid, and Aprotinin (pancreatic trypsin inhibitor--Kunitz type), all inhibitors of trypsin-like enzymes, were very effective inhibitors, as were soybean trypsin inhibitor and human alpha-1-antitrypsin. The data suggest that the tropoelastin-associated enzyme is a neutral serine protease with trypsin-like specificity.
...
PMID:Trypsin-like neutral protease associated with soluble elastin. 90 57

Bovine pancreatic trypsin was coupled to dextran after activation of the polysaccharide by cyanogen bromide. The soluble dextran-trypsin conjugated was purified by molecular sieve chromatography. After coupling, 53% of the esterase activity of trypsin remained, but the conjugate had only 7% of the caseinolytic activity of the native enzyme. The modified trypsin showed greater resistance than the native enzyme to inactivation by heat treatment, autodigestion, or denaturing agents, and was also more resistant to inhibition by trypsin inhibitors, particularly ovomucoid. Treatment with dextranase partly removed the improved stability properties and resistance to inhibition of the trypsin-dextran conjugate. The conjugated enzyme preparation consists of a heterogenous mixture of macromolecular aggregates, each containing many trypsin and many dextran molecules linked together. Intramolecular cross-linking of enzyme molecules by polysaccharide chains is considered to be responsible for stabilization of the tertiary structure of the enzyme molecules in the conjugate.
...
PMID:Preparation and characterization of a dextran-trypsin conjugate. 94 52

The coagulating activity of thrombin was increased by 120% and the esterase activity--by 100% after incubation of thrombin with factor XIII. Factor XIII also stimulated generation of thrombin in the test of two-step estimation of prothrombin. The effect, arising from the interaction of factor XIII with thrombin, was specific for this enzyme because the esterase activity of trypsin was not increased during incubation of enzyme with factor XIII under the same conditions. The data obtained suggest that factor XIII or its fragment are effectors of enzymatic activity of thrombin in vitro and in vivo.
...
PMID:[Factor XIII as a stimulator of thrombin activity]. 102 44

Amylase isoenzymes in serum, urine, saliva, jejunal juice, and pancreatic tissue were separated by isoelectric focusing. Isoamylase patterns obtained indicated that the majority of amylase activity in normal serum is of salivary gland origin. Pancreatic amylase is characteristically predominant in acute pancreatitis. The increased renal clearance of amylase in acute pancreatitis may be partly due to the increased proportion of the smaller molecular weight pancreatic amylase. However, a demonstrated increase in the renal clearance of salivary amylase in acute pancreatitis suggests a renal cause also. Autopsy pancreas samples devoid of TAME (p-tosyl arginine methyl ester) esterase activity (e.g. trypsin and plasma enzymes such as thrombin and plasmin) had isoenzyme patterns different to those samples with free proteolytic activity. Incubation of TAME esterase free pancreas with trypsin caused conversion of the former isoamylase pattern to one with the predominant isoenzymes focusing coincident with the predominant peak in serum from acute pancreatitis, jejunal aspirate, and TAME esterase positive autopsy pancreas. Such conversion suggests that pancreatic amylase is synthesized in a form different from that found in the intestinal lumen and serum.
...
PMID:Studies on serum amylase in normal man and in acute pancreatitis. 107 39

The effect of three natural trypsin inhibitors--polyvalent Kunitz inhibitor (BPTI), the inhibitor from cow colostrum (CTI) and the inhibitor from soybean (SBTI)--on esterase and kininogenase action of partially purified kallikrein preparations from human and rabbit blood serum is studied. The effect of each inhibitor was estimated from Ki values. The latters show that BPTI, SBTI and CTI are strong inhibitors of both kallikreins. Ki values, as estimated from the hydrolysis rate of N-bensoyl-L-arginine ethyl ester, were found to be for human blood serum kallikrein and BPTI, SBTI and CTI 1,1-10(-9), 4,7-10(-9) and 3,6-10(-8) M respectively and for rabbit kallikrein--1,7-10(-9), 2,3-10(-8) and 2,3-10(-8) M. In the case of kallikrein catalysing more specific kininogenase reaction Ki value for complex of human serum kallikrein with BPTI was 4,8-10(-10) M, for SBTI--1,1-10(-10) M and for CTI--3,6-10(-8) M; for rabbit kallikrein--1,7-10(-9) M, 1,1-10(-9) and 2,3-10(-8) M respectively. The data obtained suggest the high sensitivity of human and rabbit serum kallikreins to the trypsin inhibitor of peptide-protein nature and a close similarity in composition of the active site for both serum kallikreins and trypsin, two spices different kininogenases--from human and rabbit serum had also similarity in molecule conformation and composition active site.
...
PMID:[Effect of trypsin inhibitor of a peptide-protein nature on kallikreins from human and rabbit blood stream]. 108 87

Both the clotting and esterase activities of thrombin are inhibited by alpha1-proteinase inhibitor (alpha1-antitrypsin). The inhibition is a time-and temperature-dependent reaction which is proportional to the molar ratio of thrombin to inhibitor. Both the active-site serine residue of thrombin and the reactive-site lysine residue of alpha1-proteinase inhibitor are involved. alpha1-Proteinase inhibitor forms a 1:1 complex with thrombin that is comparable with the complex formed with trypsin and other proteinases. Incubation of the inhibitor with excess of thrombin, however, results in inactivation of nearly all the enzyme, even though only as much complex is formed as alpha1-proteinase inhibitor present. A portion of the remaining thrombin apparently aggregates. These results suggest that the mechanism for inhibition of thrombin may not be exactly the same as for trypsin, which is inhibited only to the extent to which complex is formed.
...
PMID:Inactivation of human thrombin in the presence of human alpha1-proteinase inhibitor. 108 57


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>

---