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)

The effect of trypsin and chymotrypsin on antibacterial factors in bovine colostrum has been studied. Endogenous complement in colostrum was extremely sensitive to both enzymes. IgM was attacked by chymotrypsin but not by trypsin. Trypsin slowly attacked IgG1, causing loss of biological activity due to cleavage of both light and heavy chains. IgG1 was only very slightly attacked by chymotrypsin. Lactoferrin and transferrin in the iron-free state were both susceptible to proteolysis, but the iron saturated forms were more resistant and tended to give rise to stable iron-binding fragments.
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PMID:The effect of trypsin and chymotrypsin on the antibacterial activity of complement, antibodies, and lactoferrin and transferrin in bovine colostrum. 74 24

As isolated from Rhodospirillum rubrum, the iron protein of nitrogenase has little or no activity. It can be activated by incubating it with a trypsin-sensitive, oxygen-labile component (activating factor) plus adenosine triphosphate and a divalent metal ion. After activation, the iron protein retains its nitrogenase activity when the activating factor is removed.
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PMID:Activating factor for the iron protein of nitrogenase from Rhodospirillum rubrum. 82 29

Living Trypanosoma musculi bloodstream trypomastigotes were agglutinated specifically with concanavalin A (ConA), wheat germ agglutinin (WGA), soybean agglutinin (SBA), and fucose-binding protein (FBP). The agglutination with these lectins of living cells from which the coat was removed by trypsinization was the same as with intact trypanosomes. Glutaraldehyde or formalin fixation did not affect the results with regard to agglutination with WGA, SBA, and FBP, but lower agglutination with ConA was observed upon fixation. By using a dense iron-dextran marker many fewer ConA marker particles were localized at the fine structural level in the intact than in trypsin-treated trypanosomes. On the basis of the results obtained by agglutination and electron microscopy, it is likely that fixation cross-links intact surface-coat components associated with the ConA binding sites. It is evident from the studies in which lectins were employed that ligands containing alpha-D-mannose, N-acetylglucosamine, N-acetylgalactosamine, and alpha-L-fucose are randomly distributed in the outer surface of the pellicular and flagellar membranes of T. musculi trypomastigotes. Results obtained with alpha-amylase- and dextranase-treated trypanosomes suggested that lectin-binding sugar ligands in the cell surface were not directly associated with alpha-1,4 or repetitive alpha-1,6 glucan-bonded polysaccharide moieties. Similar conclusions can be drawn on the basis of neuraminidase treatment with regard to N-acetylated neuraminic acids. After thorough washing, intact, but not trypsin-treated trypomastigotes were agglutinated specifically with antisera against whole mouse serum and against mouse IgG. Evidently, adsorbed constituents of mouse serum are regular components of the T. musculi surface coat. After incubation in dilute whole mouse serum or in mouse IgG solutions, also the trypsinized cells were agglutinated by the 2 antisera. No such results were obtained with trypsinized cells incubated in serum-free buffers. It was concluded that mouse serum proteins were readily readsorbed on, and firmly bound to the trypsinized cells' surfaces. Specific agglutinations were obtained with trypsinized cells after incubation in dilute rat, rabbit, bovine, and human sera and in solutions of rat and rabbit IgG in reactions with the corresponding antisera. It seems, therefore, that the host serum proteins are adsorbed nonspecifically to the cell surface of trypsinized T. musculi bloodstream forms. When examined by electron microscopy, the intact trypomastigotes were covered by an ununiform, slightly granular, fibrillar extracellular coat, applied to the entire outer lamina of the pellicular and flagellar membranes. No indication of such a coat was noted in the trypsinized organisms. Flocculent surface coat-like matrix could, however, be discerned in cells which, after trypsinization, were incubated in various sera.
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PMID:The cell surface of Trypanosoma musculi bloodstream forms. II. Lectin and immunologic studies. 93 83

Extracts of Fusarium roseum (ATCC 12822) contain an enzyme which hydrolyzes the ornithine ester bonds of fusarinine C, a cyclic trihydroxamic acid produced by this organism. The methyl ester of Ndelta-dinitrophenyl-L-ornithine is also a substrate for the enzyme, and an assay was devised using this substrate. The enzyme exhibits a sharp maximum of activity at pH 7.5 and is extremely temperature sensitive. It is strongly inhibited by HgCl2 and p-chloromercuribenzoate, and it is competitively inhibited by Ndelta-dinitrophenyl-D-ornithine methyl ester (Ki = 0.3mM). Methyl esters of glycine, L-alanine, dinitrophenyl-L-alanine, dinitrophenyl-beta-alanine, and Ndelta-dinitrophenyl-Nalpha-acetyl-L-ornithine are not substrates, although Nepsilon-dinitrophenyl-L-lysine methyl ester is as effective as the ornithine derivative. Nonspecific lipases do not hydrolyze ornithine esters, nor does trypsin. The three ester bonds of fusarinine C are progressively hydrolyzed by the enzyme to eventually yield the monomer, fusarinine. The ferric chelate of fusarinine C is not hydrolyzed. An enzyme from Penicillium sp. was isolated with identical properties toward Nbeta-dinitro-phenyl-L-ornithine methyl ester as substrate. It also hydrolyzes N,N',N"-triacetylfusarinine C, a cyclic trihydroxamate containing Nalpha-acetylornithine ester bonds, which is produced by this organism. This substrate is hydrolyzed to Nalpha-acetylfusarine. In contrast to the Fusarium enzyme, this enzyme is fully active toward the ferric trihydroxamate chelate. However, replacement of iron by aluminum leads to a completely inactive substrate. Production of the enzyme is severely suppressed by iron in the growth medium. It is proposed that these specific ornithylesterases provide a mechanism of cellular iron release by hydrolysis of the ferric ionophores, and that an iron-exchange step occurs prior to, and is a prerequisite for, hydrolysis of the ester bonds.
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PMID:Fungal ornithine esterases: relationship to iron transport. 94 72

1. The preliminary phytochemical screening of the two seeds established the presence of carbohydrates and/or glycosides, flavnoids, unsaturated sterols and/or triterpenes, saponins, trypsin inhibitors and haemagglutinins. In addition, it established the absence of cardenolides, tannins, alkaloids and oxidase enzyme. 2. Certain pharmacopoeial constants, including moisture, ash, acid-insoluble ash, water-soluble ash and crude fibre were determined. 3. The two seeds were subjected to successive extractions with different organic solvents such as petroleum ether (50-70 degrees C), diethyl ether, chloroform and ethyl alcohol. The successive yields of extractives were determined. Examination of the crude extracts showed that petroleum ether extract contained sterols and/or triterpenes, while ether, chloroform, and ethyl alcohol extracts contained reducing substances. 4. General analysis of the two seeds for proteins, fats, carbohydrates, fibre and ash contents were carried out and the results were given in g/100 g dry seeds. Pigeon pea contained 25.2 g protein, 170 mg calcium and 8.9 mg iron. The protein content of kidney bean was 23 g, while calcium and iron contents were 134 mg and 8.02 mg respectively. 5. Extractions of the proteins using different solvents such as cold water, hot water, saline buffer pH 7 and sodium hydroxide was the best extractant. 6. The amino-acid content of the two seeds, whether raw or cooked, showed that they were deficient in methionine, cystine and tryptophan. Other essential amino acids were present in amounts higher than that given by the FAO provisional pattern. 7. Cooking the seeds by the popular methods used in the country resulted in an increase in the amounts of the amino acids, threonine, leucine and isoleucine, while the other amino acids present remained unchanged or decreased. It was also observed that cooking the seeds destroyed the trypsin inhibitors and haemagglutinins found in the two seeds.
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PMID:Phytochemical and nutritional studies on pigeon pea and kidney bean cultivated in Egypt. 96 10

The iron-saturated and iron-free (apo) forms of bovine transferrin and lactoferrin were digested with trypsin and the digests analysed by column chromatography and electrophoresis. Both of the iron-saturated proteins were more resistant to proteolysis than the corresponding apoproteins, and iron-transferrin was more resistant than iron-lactoferrin. Digestion of iron-transferrin yielded two iron-binding fragments with molecular weights of 32 000 and 38 500 whereas apotransferrin yielded only the larger fragment. In digests of lactoferrin, up to five different fragments with molecular weights ranging from 25 000 to 52 700 were detected, there being no obvious qualitative difference between digests of iron-lactoferrin and apolactoferrin. The susceptibility of apolactoferrin to tryptic digestion was only slightly reduced when apolactoferrin was complexed with beta-lactoglobulin, suggesting that complex-formation is not a mechanism for protecting lactoferrin against intestinal degradation. There was no immunological cross reaction between bovine transferrin or its digestion products against anti-lactoferrin antiserum, or vice-versa.
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PMID:The effect of trypsin on bovine transferrin and lactoferrin. 97 13

1. The proximate analysis of raw Syrian lentils (Lens esculentus), variety red chick pea (Cicer arietinum) variety balady, has been made. The protein content of the two raw seeds were 23 and 22 g% for lentils and chick peas, respectively. Ethereal extract, fiber, ash, calcium, phosphorus and iron content of the two raw seeds have been also assayed. 2. The levels of most of the amino acids were also estimated in the raw and cooked seeds. It was found that tryptophan- and sulphur-containing amino acids were the most limiting ones. Cooking the seeds by the same methods commonly used in Syria resulted in the loss of most of the amino acids, with the exception of lysine and tryptophan which were slightly increased. 3. Trypsin inhibitors and saponins were detected in the raw seeds. Haemagglutinins were present in raw lentils only. Cooking the seeds destroyed the trypsin inhibitors and haemagglutinins and did not affect the saponins. 4. The net protein utilization of whole lentils and chick peas were 38 and 53, respectively. Decortication of lentils or cooking without decortication has no effect on the NPU values. Cooking the decorticated lentil seeds raised its NPU values from 38 to 56. Cooking chick peas resulted in a slight increase in their NPU. Supplementation of the raw and treated seeds with methionine and tryptophan raised its NPU values markedly.
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PMID:Nutritive studies on some raw and prepared leguminous seeds commonly used in the Arab Republic of Syria. 102 Mar 73

The effect of trace metals on plasma alpha1-antitrypsin was studied in vitro by adding known concentrations of trace metals, either alone or in combination, to plasma. Cadmium was the only trace metal that reduced the concentration of alpha1-antitrypsin and depressed the trypsin inhibitory capacity. No such effects were found with divalent lead, mercury, nickel, iron, and zinc ions. The present study appears to offer a plausible explanation for the emphysema that occurs in industrial workers exposed to cadmium.
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PMID:Influence of cadmium and other trace metals on human alpha1-antitrypsin: an in vitro study. 108 68

During the year 1974, 111 patients with urticaria were studied in the Department of Dermatology, of the Saint Paul's Hospital (Autonomous University of Barcelona). Among those, 77 had chronic urticaria, of which 22 a had low blood iron values. After iron treatment the urticaria improved or was cured in some of these patients. The remaining cases in which the cause of their hives was unknown were followed for one year. Some systemic causatives for their urticaria may appear on longer follow-up. At the same time, blood levels of salicylates trypsin and alpha-chymotrypsin were checked in 14 patients, with the object of a possible relationship concerning the persistence of the urticaria.
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PMID:[Chronic urticaria and serum iron]. 124 Oct 79

The surface coat of syncytial trophoblast from term human placentas was studied using cytochemical methods (colloidal iron, alcian blue-lanthanum nitrate, dialyzed iron) in coordination with tissue enzyme digestions (trypsin, neuraminidase) and sialic acid analyses. The presence of at least two highly acidic anionic components that contribute significantly to the surface negativity of trophoblast has been demonstrated. The first of these, sialic acid, was removed with neuraminidase. Tissue digestion with this glycosidase was accompanied by a decrease in trophoblast surface staining with colloidal iron, a decrease in tissue sialic acid, and an increase in the concentration of sialic acid in the incubating medium. Results from methylation experiments were consistent with the presence of sialic acid. The second anionic component(s) was identified by removal with trypsin of a glycocalyx constituent that stained with both colloidal iron and lanthanum. After trypsinization, tissue sialic acid levels were not significantly different from control values, and no detectable sialic acid was present in the incubating medium. The identity of this anionic component has not been established. Both sialic acid and nonsialic acid acidic components are distributed in higher density on membrane of microvilli than on intermicrovillous surface membrane. In addition, the sialic acid moieties appear to be clustered in the glycocalyx.
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PMID:The nonuniform distribution of acidic components on the human placental syncytial trophoblast surface membrane: a cytochemical and analytical study. 124 83


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