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)

Fresh human skin extract made in salt solution after a prior buffer extraction was shown to enhance the hydrolysis of N-alpha-benzoyl-DL-arginine beta-naphthylamide (BANA) by trypsin. This trypsin enhancing effect was further shown to be both stabilizing and activating. After chromatography on Sephadex G-100, the trypsin binding factor was found in fractions of void volume. Protease binding took place in physiological and hypotonic but not in hypertonic NaCl-solutions (0.5 mol/l). The proteinase binding factor was further purified by trypsin-Sepharose 4 B affinity chromatography. It was found to bind also chymotrypsin and elastase and to be thermostable (100 degrees C for 20 min), precipitable at acidic pH (3.5), and by acetone and ammonium sulphate (60% saturation). The bound proteinases were found to preserve their hydrolytic activity towards protein substrates. Bound trypsin and chymotrypsin could completely be inhibited by soybean trypsin inhibitor. The binding factor did not react with anti-human-alfa2-macroglobulin antiserum from rabbit.
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PMID:Proteinase binding and enhancing factor from human skin. 46 38

EDCl is a novel glycoprotein, mol wt 27,000, isolated in 1976 from leukemic urine. It inhibits the serine proteases trypsin and chymotrypsin and is antigenically related to interalpha trypsin inhibitor (IATI), mol wt 170,000, a normal plasma antiprotease. Since psoriasis is a non neoplastic hyperproliferative state, we have now measured EDCl by a specific radioimmunoassay (RIA) in plasma and urine of 24 untreated psoriatic patients. EDCl was not detectable in normal urine (less than 1 mg/gm creatinine) or plasma (less than 1 mg/L). 55% of psoriatic urine specimens were positive by RIA, containing 8 to 110 mg/gm creatinine. 75% of plasmas were positive, containing 12 to 32 mg/L. Plasma and urine contents of EDCl were significantly (P less than .05) correlated with severity of clinical disease (% skin involved) but not with age, sex, distribution or type of lesion, family history or arthritis.
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PMID:Accumulation of urinary cancer-related glycoprotein, EDCl, in psoriasis. 47 29

1. The Bowman-Birk soya-bean trypsin inhibitor (BBTI) begins to cause pancreatic enlargement and increased enzymic activity in the pancreas of chicks after a minimum of 7 d of feeding. 2. The active inhibitory site of BBTI against trypsin is the factor involved in the pancreatic enlargement and increase of pancreatic enzyme activity in chicks.
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PMID:Kinetics of native and modified Bowman-Birk soya-bean trypsin inhibitor on growth and enzymes activities of the chick pancreas. 48 87

The amino acid sequence of the A- and B-chains of porcine pancreatic kallikrein B is presented and compared to that of porcine trypsin. The overall homology between both enzymes is 37% identical residues in corresponding position and 51% chemically similar resideus. Comparison of the sequences with the crystal structure of bovine trypsin reveals that the trypsin "autolysis loop" is enlarged in kallikrein by two residues but lacks the basic residue at the cleavage site. Substitutions at the calcium-binding site of trypsin which include Arg 70 for Glu 70 possibly interfere with ion binding. Insertions between trypsin residues 95 and 96 obviously form a new kallikrein "autolysis loop" containing the site of cleavage between the A- and B-chains. One carbohydrate moiety is attached to this surface loop at Asn 95, the second to Asn 239 at the same edge of the globular molecule. The residues at the surface of the substrate binding site are substituted to an extent of 85% while the residues forming contacts to the trypsin inhibitor (Kunitz) are highly preserved. Immunodiffusion studies as well as identity of the N-terminal sequences of pancreatic, submandibular and urinary kallikrein reveal the same genetic origin of the three glandular kallikreins.
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PMID:The primary structure of porcine glandular kallikreins. 49 14

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

The activity of amylase, lipase and trypsin was increased and that of the trypsin inhibitor decreased in the blood serum of young peptic ulcer patients as compared with healthy persons. The antiulcerous dietetics normalized significantly the parameters studied. Similar highly pronounced shifts in the activity of the blood pancreatic enzymes were revealed in atrophic gastritis patients. Hyperamilasuria and clinical symptoms of pancreatitis were not observed both in the peptic patients, and in the atrophic gastritis patients. The shifts in the blood content of pancreatic enzymes and their dynamics correlated mainly with the intensity and dynamics of the disturbances in the locomotive function of the gastroduodenal system.
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PMID:[Effect of the alimentary factor on certain indices of the functional state of the pancreas in young peptic ulcer patients and atrophic gastritis patients]. 51 99

Four proteinase inhibitors, A-II, A-III, B-I, and B-II, were isolated from seeds of Albizzia julibrissin (silk tree) of the subfamily Mimosoideae, which is often regarded as the most primitive group of the Leguminosae plants. They were all of the high-molecular weight type (21,600 for A-II and A-III, and 19,000 for B-I and B-II), and composed of two polypeptide chains, linked together by a disulfide bond. A-II (A-III) inhibited bovine trypsin and alpha-chymotrypsin probably at an identical site. B-I (BII) inactivated bovine alpha-chymotrypsin and porcine elastase. Sequence analyses of A-II and B-II revealed a considerable homology with soybean trypsin inhibitor (Kunitz) but suggested the presence of an about 20-amino acid insertion in the A-II molecule.
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PMID:Proteinase inhibitors from a mimosoideae legume, Albizzia julibrissin. Homologues of soybean trypsin inhibitor (Kunitz). 52 39

In the present study, we separated and partially purified brown substances from eggplants and examined their inhibitory action on trypsin activity. The following results were obtained: 1. The first half of the elute after passing ethanol-extractable brown substances through DEAE-cellulose column showed no inhibitory action on trypsin, whereas the middle portion of the elute contained a trypsin inhibitor(s). Similar results were obtained after fractionation with Sephadex G-25. The degree of inhibition was increased after purification. 2. Both crude ethanol extracts of eggplant brown substances and acetate buffer extracts from eggplant exocarps showed similarly an enzyme inhibition of competitive type. 3. Both nondialyzable portion of ethanol extracts and purified fraction after Sephadex G-25 passage showed a noncompetitive type of inhibition. DOPA-melanin and chlorogenic acid-melanin as model substances exhibited a similar noncompetitive inhibition. Purified ethanol extracts of eggplant brown substances showed an ultraviolet absorption spectrum similar to that of chlorogenic acid. From these findings it is concluded that both eggplant brown substances and polyphenol substances play an essential role in the inhibition of digestive enzymes.
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PMID:[Influence of food browning on nutrition. III. Effect of brown substances on digestive enzyme activity (author's transl)]. 54 14

Sixty-eight growing gilts with a 12 kg average initial weight were used in seven trials to study the effect of dietary raw soybean (Harosov) and SBTI (Kunitz soybean trypsin inhibitor) on pancreatic and small intestinal trypsin and chymotrypsin activities. A solvent-extracted, heated soybean meal (SBM) was used, cause reduced growth. Both a single-meal and continuous feeding of the raw soybean diet caused a decrease in the pancreatic trypsin and chymotrypsin activities. In contrast, to the rat and the chick, the pancreas of the pigs did not enlarge subsequent to consumption of the raw soybean or SBTI diets. Raw soybean feeding also resulted in an inhibition of the intestinal trypsin and chymotrypsin activities. This inhibiting effect was greater than that of the SBTI, especially the chymotrypsin-inhibiting effect. This suggested that soybean constituents other than the SBTI, such as the Bowman-Birk inhibitor, caused inhibition. In the pig the inhibition of the intestinal proteolysis may be a major cause of reduced growth when raw soybean is fed.
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PMID:Effect of dietary raw soybean and soybean trypsin inhibitor on trypsin and chymotrypsin activities in the pancreas and in small intestinal juice of growing swine. 55 60

Five trypsin and alpha-chymotrypsin inhibitors which have low molecular weights (ranging from 6800 to 8600) and are present in soybean seeds of the Tracy variety have been isolated and purified, and single crystals which give x-ray diffraction data beyond 3-A spacings have been obtained from one of them. The trypsin inhibitor crystallizes in a monoclinic unit cell of symmetry P2(1) and dimensions a = 25.919(7) A, b = 43.23(1) A, c = 19.905(5) A, and beta = 103.63(2) degrees. The assymmetric unit contains 1 molecule of molecular weight 6800. The crystal, which has been found to be unusually stable to x-radiation, has solvent content of approximately 26% by volume.
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PMID:A soybean trypsin inhibitor. Crystallization and x-ray crystallographic study. 55 36


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