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)

Conditions are described for the production of large amounts of an extracellular elastolytic protease by Vibrio vulnificus. The yield of enzyme was maximal during the late exponential growth phase and was stable during the stationary growth phase in a medium composed of 2% Proteose Peptone and 1.5% NaCl. The protease has a molecular weight of ca. 50,500 (estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis), an isoelectric point of ca. 5.8, and a pH optimum range against azocasein and elastin of pH 7 to 8. The caseinolytic and elastase activities in protease preparations partially purified by ammonium sulfate precipitation were inseparable by gel filtration, hydrophobic interaction chromatography, and isoelectric focusing. Both activities were deleteriously affected by heat, low pH, heavy-metal ions, chelating agents, reducing agents, sodium cyanide, N-bromosuccinimide, alpha-2-macroglobulin, and phosphoramidon, but were unaffected by various trypsin inhibitors, chymostatin, aprotinin, leupeptin, pepstatin A, phenylmethylsulfonyl fluoride, and N-ethylmaleimide.
...
PMID:Production and partial characterization of an elastolytic protease of Vibrio vulnificus. 390 48

Murinoglobulin, a newly identified mouse plasma protein with trypsin-protein esterase activity (Saito, A. & Sinohara, H. (1985) J. Biol. Chem. 260, 775-781), was also found in rat plasma and purified to apparent homogeneity. The serum level of rat murinoglobulin was 14.1 mg/ml, amounting to 1/3 of the total serum globulin fraction. Rat murinoglobulin was a monomeric glycoprotein (Mr = 210,000) containing 12% carbohydrate. Rat plasma contained two isoforms of murinoglobulin, termed I and II, which showed complete immunological identity on double diffusion analysis using rabbit antiserum raised against isoform I or II. These antisera also showed partial cross-reactivity towards mouse murinoglobulin and rat alpha-1-macroglobulin but not towards rat or human alpha-2-macroglobulin. The chemical compositions, peptide mapping patterns and electrophoretic mobilities of the two isoforms resembled each other but clearly differed from those of rat alpha-1- or alpha-2-macroglobulin. Rat murinoglobulin inhibited the proteolytic activity of trypsin towards casein and remazol brilliant blue hide powder. The inhibition as to the latter substrate was greater than that as to the former. When molar ratios of inhibitor to trypsin were low, murinoglobulin and the two alpha-macroglobulins stimulated the amidolytic activity of trypsin towards a synthetic substrate. At higher ratios, however, murinoglobulin, but not the alpha-macroglobulins, inhibited the same activity. The trypsin-protein esterase activity of murinoglobulin and the two alpha-macroglobulins was impaired by a molar excess of soybean trypsin inhibitor. Murinoglobulin and the two alpha-macroglobulins were inactivated by methylamine with a concomitant unmasking of the thiol group. Murinoglobulin was much more sensitive to soybean trypsin inhibitor and methylamine than the two alpha-macroglobulins.
...
PMID:Rat plasma murinoglobulin: isolation, characterization, and comparison with rat alpha-1- and alpha-2-macroglobulins. 393 48

The most abundant glycoprotein in the coelomic fluid of sea urchin Anthocidaris crassispina was purified and its subunit structure, molecular form in the native state, amino acid composition, and electron micrographic image were studied. The results showed that the protein in its native state was basically a tetramer with a total molecular weight of about 700,000, which was in equilibrium with a high molecular weight form corresponding to an octamer. The electron micrograph of the tetramer showed two ellipsoidal units aligned in parallel with a wide gap in between. The subunits all had the same molecular weight of 180,000 +/- 10,000 and were disulfide bonded in pairs. The carbohydrate content was about 16% with mannose and fucose as the two most abundant sugars. Although this protein accounted for 70% of the total protein in the coelomic fluid, it did not take part in the known activities of the fluid, namely hemagglutination and coagulation. Despite its structural similarity to the mammalian alpha-2-macroglobulin or reptilian and avian ovomacroglobulins it did not interact with bovine trypsin or chymotrypsin. This protein showed immunological cross reactivity with 23S glycoprotein purified from sea urchin eggs which, we believe, corresponds to the previously described 22-27S protein particles in eggs.
...
PMID:Purification of the most abundant protein in the coelomic fluid of a sea urchin which immunologically cross reacts with 23S glycoprotein in the sea urchin eggs. 404 50

Normal animal sera inhibit at least one Clostridium histolyticum proteinase. An assay procedure based on immune hemolysis was developed for the estimation of this inhibition. This inhibitory activity occurs in various levels in the sera of different animal species. The highest titers have been obtained with rat sera. The inhibitory activity from human serum was isolated and purified 16- to 27-fold by Sephadex G-200 gel filtration and diethylaminoethyl cellulose or hydroxylapatite chromatography. The properties of the human serum inhibitor of the clostridial proteinase were compared with a trypsin inhibiting factor found in the partially purified preparations. Identical behavior of the two inhibitory factors was observed when measured by heat inactivation, beta-mercaptoethanol sensitivity, pH stability, and sucrose gradient centrifugation. The inhibitory factor has an approximate sedimentation coefficient (S(20,w)) of 17. Goat anti-alpha-2-macroglobulin specifically precipitated the clostridial proteinase inhibitor from a partially purified preparation.
...
PMID:Characterization of a human serum inhibitor of Clostridium histolyticum proteinase(s). 530 20

Alpha-2-macroglobulin (alpha 2-M) has been purified from the plasma of patients with cystic fibrosis and normal controls, and the proteolytic subunit cleavage on reaction with trypsin has been compared. As no differences were observed between the two groups, a primary genetic defect affecting alpha 2M subunit cleavage in cystic fibrosis is unlikely.
...
PMID:Normal subunit cleavage of alpha-2-macroglobulin in cystic fibrosis. 615

Serum trypsin, total trypsin-inhibitor capacity, alpha-1-antitrypsin and alpha-2-macroglobulin were analyzed daily in ten patients hospitalized as a result of acute pancreatitis. Markedly raised serum trypsin concentrations were found in all patients. Alpha-1-antitrypsin and the trypsin-inhibitor capacity were also significantly increased as compared to post-illness values, but alpha-2-macroglobulin tended to decrease during acute pancreatitis. The post-illness values of all these parameters were in the normal range. It is concluded that a deficiency of alpha-1-antitrypsin, trypsin-inhibitor capacity of alpha-2-macroglobulin is not present in patients with acute pancreatitis which could render the pancreas more vulnerable to its own proteases. During acute pancreatitis trypsin is released into the circulation, but it is effectively inactivated by serum protease inhibitors, mainly alpha-1-antitrypsin, which can be seen as an increased trypsin-inhibitor capacity in these patients. The use of protease inhibitors in the treatment of acute pancreatitis seems to be unnecessary against this background. Increased serum trypsin values can be used when confirming the diagnosis of acute pancreatitis.
...
PMID:Serum immunoreactive trypsin and trypsin inhibitors during acute pancreatitis. 616 88

Proteolytic enzyme inhibitor activity has been measured in the rheumatoid knee by 2 different techniques. The inactivation rate of trypsin injected into the joint in 13 patients was compared with synovial fluid levels of alpha-1-antitrypsin (apha 1AT), alpha-2-macroglobulin (alpha 2M) and trypsin inhibitory capacity (TIC). The lack of correlation and the fact that an inverse relationship was shown between the T1/2 to inactivation and joint damage suggests that additional mechanisms are involved in the inactivation of destructive enzymes. Serum levels of alpha 1AT and TIC were elevated in 36 rheumatoid arthritis (RA) patients when compared with control values and RA synovial fluid inhibitor levels elevated by comparison with osteoarthritic figures. The synovial fluid alpha 1AT and TIC correlated with the activity of the lysosomal enzyme beta-acetyl glucosaminidase (beta AGA) but only trace amount of neutral protease activity was detected probably because of the large concentration of inhibitors present. The deficient Pi phenotype MZ was rarely encountered.
...
PMID:Antitrypsin activity and enzyme inhibitors in the rheumatoid joint. 617 Jul 54

Synovial tissue from patients with rheumatoid arthritis, systemic lupus erythematosus, osteoarthritis, and having menisectomies was examined by immunofluorescence for deposits of alpha-2-macroglobulin (alpha 2M). In inflammed tissues, alpha 2M was found in the synovial lining cells and in perivascular cells. The amount of alpha 2M correlated with the degree of inflammation. Similarly, free lining cells obtained by trypsination of the intact synovial membrane contained identical inclusions. alpha 2M was not detected in the menisectomy cases and in the less inflammatory osteoarthritic specimens. In-vitro studies demonstrated uptake of alpha 2M-trypsin complexes but not of native alpha 2M by most of the cultured synovial cells whether they came from rheumatoid patients or controls. The internalised complexes disappeared within 12 hours of culture. The results suggest that alpha 2M-proteinase complexes formed in the joint are taken up by phagocytic and perivascular cells in a similar way to immune complexes.
...
PMID:Deposits of alpha 2M in the rheumatoid synovial membrane. 618 47

20 series of alpha-2-macroglobulin (alpha 2-M) preparations with a specific activity of 15 +/- +/- 1 IU/mg were obtained by means of semi-industrial fractionation of human blood plasma Kohn 111 residue including polyethylene glycol and ethanol treatment. The preparations obtained inhibited proteolytic enzymes of fibrinolytic, kinin and blood coagulation systems as well as plant and bacterial proteinases. After intravenous administration of the alpha 2-M preparation into rats at a dose of 850-11,000 IU/kg the globulin concentration was correspondingly increased by 23-25% in blood. The half-time of excretion of the alpha 2-M therapeutic dose (2,700-5,700 IU/kg) was about 6.6-13,9 hrs which was 9-20-times higher as compared with the corresponding value for contrical. In the experimental proteolysis (effect of trypsin at a dose of 470-6,670 KU/kg) preparation of alpha 2-M, administered at a dose of 2,000-6,000 IU/kg, exhibited a distinct antiprotease action with a 1.5-1.7-fold increase in the rate of inactivation and excretion of trypsin. The alpha 2-M preparation was shown to be highly effective in prophylactic treatment. The advantages of antiprotease drugs based on human alpha-2-macroglobulin are discussed.
...
PMID:[Experimental study of the antiproteinase activity of human alpha-2-macroglobulin concentrate]. 619 17

Various strains of black-pigmented Bacteroides species were grown on horse blood agar and suspended in human serum. After various times of incubation the effect of the bacteria on the serum was evaluated by polyacrylamide gel electrophoresis and "rocket" immunoelectrophoresis. The formation of trichloroacetic acid-soluble material in the suspensions and the capacity of the treated sera to inhibit the activity of trypsin were also determined. The two tested strains of Bacteroides gingivalis (W83, H185) degraded most serum proteins, including the plasma proteinase inhibitors alpha-1-antitrypsin and alpha-2-macroglobulin. They did not, however, degrade alpha-1-antichymotrypsin. Bacteroides intermedius NCTC 9336, Bacteroides asaccharolyticus NCTC 9337, and an asaccharolytic oral strain different from B. gingivalis (BN11a-f) did not degrade the plasma proteinase inhibitors. These strains were, however, able to inactivate the capacity of serum to inhibit the activity of trypsin.
...
PMID:Degradation of the human proteinase inhibitors alpha-1-antitrypsin and alpha-2-macroglobulin by Bacteroides gingivalis. 619 82


<< Previous 1 2 3 4 5 6 Next >>

---