Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Tissue extract of antrochoanal polyps showed a faint lysis area on standard fibrin plates, but streptokinase (SK)-added tissue extract showed a large lysis area. No fibrinolytic activity was observed on plasminogen-free fibrin plates. It is concluded, therefore, that the fibrinolytic activity observed after SK addition is indicative of the existence of SK-responsive protein proactivator. The tissue extract did not contain plasminogen or antiprotease against trypsin or papain. It was stable at neutral pH at 37 degrees C and stable at acid pH at 70 degrees C. The role of proactivator is discussed in relation to the growth or enlargement of antrochoanal polyps.
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PMID:A protease-antiprotease system in antrochoanal polyp. I. Evidence for the existence of proactivator. 39 30

Purified Streptomyces albus lytic enzyme was used in an attempt to extract type-specific antigen from a type 1, group A streptococcus. The presumably type-specific antigen was purified by ammonium sulfate fractionation followed by chromatography on O-(carboxymethyl)-cellulose columns. Comparison of the enzyme-extracted substance with acid-extracted material showed it to be serologically different from M protein. In addition, the extract obtained by enzyme treatment was resistant to trypsin as well as to the lytic enzyme. It was inactivated partially by pepsin and totally by papain. Comparison of the enzyme extract with pepsin-extracted T antigen showed these two preparations to be serologically identical. Subtle differences in their susceptibility to heat and acid treatment were noted. Immunodiffusion analyses of acid-extracted M protein and pepsin-extracted T protein, as well as with the enzyme extract, clearly established that the M-protein preparation contained a component serologically identical with one of the precipitinogens common to the other two extracts.
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PMID:Comparison of Streptomyces albus muramidase-extracted streptococcal antigen with acid-extracted M antigen and with pepsin-extracted T antigen. 40 3

The electrophoretic mobilities of rough and smooth microsomes were studied using free electrophoresis in a sucrose gradient. Rough microsomes have a higher net negative surface charge but removal of the ribosomes decreases their mobility to that of smooth microsomes. Treatment with neuraminidase and phospholipases C and D does not affect the mobility of total smooth microsomes, but this mobility is increased by approximately 20% after trypsin and papain treatment and by approximately 12% after phospholipase A treatment. Further treatment of trypsin-digested smooth microsomes with phospholipase C re-establishes the original mobility. This effect is not caused by the removal of lipid phosphate groups, but by the liberation of negatively charged protein species that are normally buried under trypsin-sensitive proteins. Low concentrations of trypsin also solubilize enzyme proteins from smooth liver microsomes of phenobarbital-treated rats, but the electrophoretic mobility is not increased, indicating structural differences between induced and control membranes.
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PMID:Electrophoretic mobility of microsomes from rat liver. 40 61

Antigen was partially purified from Neisseria gonorrhoeae B370 saline wash and used to assay human sera for the presence of antibodies to N. gonorrhoeae. The antigen activity as monitored by counterimmunoelectrophoresis (CIE) is resistant to trypsin and papain but sensitive to heat and periodate oxidation. Of the sera from patients with bacteriologically confirmed cases of gonorrhea, 80% were positive by CIE using this antigen preparation. Of the sera in the negative control group 11% were reactive.
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PMID:Detection of antibodies to Neisseria gonorrhoeae by counterimmunoelectrophoresis. 41 47

The ability of detergents (Triton X-100 and deoxycholate), high ionic strength solution (3 M KC1), and proteolytic enzymes (papain and trypsin) to solubilize human thyroid microsomal antigen was studied. Antigenic activity released from thyroid microsomal preparation into the incubation mixture was separated by centrifugation at 143,000 x g for 90 min and measured using 125I-labeled human immunoglobulin G (IgG) with elevated antimicrosomal (anti-M) and undetectable anti-thyroglobulin antibodies (anti-M IgG). All solubilized materials were shown to bind [125I]anti-M IgG and to inhibit its binding to untreated thyroid microsomes. These effects were specific and dose related. Measurements of specific activity and total amount of solubilized antigen by an absorption technique showed that Triton X-100 was the most effective agent, followed by deoxycholate, papain, trypsin, and 3 M KC1 in decreasing order. Affinity chromatography with the deoxycholate-solubilized material coupled to Sepharose 4B resulted in a 15.6-fold purification of [125I]anti-M antibodies. The present results indicate that thyroid microsomal antigen may be solubilized by several agents and this can provide the basis for its identification and purification.
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PMID:Solubilization of human thyroid microsomal antigen. 42 74

The inactive 50,000-dalton fragment of human plasma alpha1-proteinase inhibitor resulting from limited proteolysis of the inhibitor by Crotalus adamanteus proteinase II has been isolated and partially characterized. The amino acid composition of the inactivated inhibitor indicates the loss of a peptide fragment from the intact inhibitor. Both intact and inactivated inhibitor contain COOH-terminal lysine. However, the NH2 terminus of the intact inhibitor is Glx, whereas that of inactivated inhibitor is methionine. NH2-terminal analysis of the inactive inhibitor fragment revealed the following sequence: -Met-Phe-Leu-Glu-Ala-Ile-Pro-Met-Ser-Ile-Pro-Pro-Gln-Val-Lys-Phe-Asn. The data show that the venom proteinase has inactivated alpha1- proteinase inhibitor by cleavage of a single bond which differs from that reported for trypsin or papain.
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PMID:Characterization of the inactive fragment resulting from limited proteolysis of human alpha1-proteinase inhibitor by Crotalus adamanteus proteinase II. 44 52

Glia maturation factor from the pig brain can be detected in two molecular forms: the high molecular weight form which is 200 000 dalton in size and the low molecular weight form which is 40 000 dalton in size, as determined by Sephadex gel filtration. The former accounts for 85% of the total biological activity extracted at physiologic pH. The proportion of the low molecular weight form increases following freeze-thawing and ion-exchange chromatography. In addition to the morphological effects, both forms possess mitogenic activity but no esteropeptidase activity. Both forms show similar enzyme susceptibility, being inactivated by papain, ficin and pronase but resistant to subtilisin, thermolysin and trypsin. The high molecular weight form is more resistant to denaturation by low pH, heating and urea than the low molecular weight form. The high molecular weight factor has an isoelectric point of 4.27 whereas the low molecular weight factor has one of 5.04.
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PMID:Multiple molecular forms of glia maturation factor. 46 31

In order to elucidate receptors of proteolytic enzyme-treated red cells which react with Phaseolus coccineus L. lectin, the receptors prepared by affinity chromatography were serologically investigated. P. coccineus lectin had high agglutinin activity for bromelin-, papain- and pronase-treated red cells but that for the cells treated with ficin and trypsin was relatively low. Analyses of chemical composition revealed that sialic acid of the receptors from normal red cells was considerably much as compared with that from the treated cells. On the contrary, the enzyme treatment did not affect particularly carbohydrate composition of the receptors. Disc electrophoresis showed that the patterns of receptors from red cells treated with bromelin or papain were different from those from the other cells. On two-dimensional immunoelectrophoresis, the receptor of trypsin-treated cells gave five precipitation lines against anti-stroma and that of papain-treated cells three lines, but any other receptors showed no line. These findings indicate that there are plural receptors for P. coccineus lectin in red cells treated with each of proteolytic enzymes and that the receptors from respective red cells have electrophoretically and serologically different property.
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PMID:On the receptors of human red cells reacting with Phaseolus coccineus L. lectin. 49 65

A trypsin inhibitor was isolated and purified from the bran of rice, Oryza sativa, by extraction with 1% sodium chloride, heat treatment, ammonium sulfate precipitation, ion-exchange chromatography on a CM-Sephadex C-25 and gel filtration on a Sephadex G-75. The final preparation was homogeneous by electrophoretic analysis. Rice bran trypsin inhibitor (RBTI) had a molecular weight of about 14,500 and an isoelectric point of 8.07. The amino acids, acid composition was characterized by high contents of basic amino acids, aspartic acid, glutamic acid, proline and cystine. BRTI inhibited bovine trypsin at an inhibitor-enzyme molar ratio of 1:1.6. It displayed, however, nobility to inhibit alpha-chymotrypsin, pepsin, papain and subtilisin BPN'.
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PMID:Purification and characterization of a trypsin inhibitor from rice bran. 50 53

Four bacteriocins of L. fermenti, 3 bacteriocins of L. brevis and 1 bacteriocin of L. buchneri were studied with respect to morphology of the inhibition growth zones of the indicator strains, capacity for diffusion through cellophane, sensitivity to high temperature, bacterial proteases, trypsin, chymotrypsin, pepsin, papain, nucleases and lysozyme. According to the differences in their properties the bacteriocins were classified as belonging to 8 types, including 4 types of L. fermenti bacteriocins and 3 types of L. brevis bacteriocins.
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PMID:[Bacteriocin properties of Lactobacillus fermenti, Lactobacillus brevis and Lactobacillus buchneri]. 50 77


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