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

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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 primary structure of rat liver microsomal glutathione transferase has been determined. The 14C-carboxymethylated protein was fragmented with CNBr and proteolytic enzymes. The basis of the analysis was information from sequenator degradations of the intact protein, the largest CNBr fragment, and a large COOH-terminal fragment derived from a digest with Glu-specific staphylococcal protease. Remaining, smaller fragments were analyzed with the manual dimethylaminoazobenzene isothiocyanate method. Pepsin and limited acid hydrolysis were used to obtain peptides to confirm and overlap hydrophobic structures in the COOH-terminal half of the protein where trypsin and chymotrypsin failed to give any cleavage. Combined, these data permit the deduction of a 154-residue amino acid sequence. No evidence for micro-heterogeneity was obtained. The NH2-terminal alanine residue has a free alpha-amino group and the cysteine residue involved in activation of the enzymatic activity by sulfhydryl reagents is at position 49. The protein chain contains three regions with predictions for long beta strand secondary structures (positions 11-26, 103-120, and 131-145). Predictions may be inaccurate in membrane-associated proteins, but two of these regions also affect the three most hydrophobic segments. Thus, residues 11-35 form a long, largely hydrophobic part interrupted by only one charged residue (Lys-25), and residues 81-97 and 114-126 constitute the most hydrophobic segments directly noticeable from the hydrophilicity curve of the protein chain. These special parts of the molecule are of interest in relation to membrane interactions.
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PMID:Microsomal glutathione transferase. Primary structure. 393 48

The Streptococcus mutans group b antigen of strain FA1 has been defined as to chemical composition and immunological specificity. The antigen in cold trichloroacetic acid extracts was fractionated on diethylaminoethyl-Sephadex A-25 at pH 8.5. Two forms were isolated: a polysaccharide and a mucoprotein. The two polymers reacted as a single substance in agar gel diffusion against specific adsorbed FA1 rabbit antisera but were separated by gel immunoelectrophoresis. No reaction with any other S. mutans or streptococcal group sera occurred. Galactose composed about one-third and galactosamine about 3% of the total weight of each polymer. Rhamnose was a major component of the polysaccharide (47%) but was present only in traces in the mucoprotein. The protein content of the latter was about 40%. No significant quantities of glycerol, phosphorus, or muramic acid were present in either case. Pepsin and trypsin had no effect on the serological specificity of the mucoprotein. d-Galactose and d-galactosamine were strong inhibitors (70%) of the precipitin reaction, whereas d-glucose, d-glucosamine, and N-acetyl-d-glucosamine inhibited between 25 and 35%. The results indicate that the antigen is a major antigenic component of the cell wall and that the specificity of the antigen resides in binding sites which contain both d-galactose and d-galactosamine. Agglutination of whole cells by specific group b antiserum indicates the antibody receptor sites of the polysaccharide antigen are at the surface of the streptococcal cell. The mucoprotein, but not the polysaccharide, was released from the cell by lysozyme. Lysis did not occur. The immunological specificity and other characteristics of the antigen establishes it as the identifying antigen of S. mutans group b.
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PMID:Structure and immunological specificity of the Streptococcus mutans group b cell wall antigen. 412 3

1. With the aid of a coupled system involving glutathione reductase, the reaction of glutathione with the disulphide bonds of purified proteins has been studied. 2. Bovine serum albumin, conalbumin, lysozyme, trypsin inhibitors from egg white, lima bean and soya bean either did not react with glutathione or reacted only slightly. With these proteins reactivity was markedly increased by limited proteolysis. 3. Bovine and human gamma-globulins, fibrinogen and beta-lactoglobulin exhibited some reactivity (less than 15%) with glutathione and again this was increased by limited proteolysis. Pepsin, trypsin and chymotrypsin exhibited greater reactivity than the proteins previously mentioned. Di-isopropylphosphoryl-chymotrypsin exhibited less reactivity than chymotrypsin, suggesting that autolysis under the experimental conditions used contributed towards the reactivity of this protein. Proteolysis also increased the reactivity of these proteins. The three disulphide bonds of insulin were reduced by glutathione. 4. Above 35 degrees the disulphide bonds of serum albumin show a progressive increase in reactivity and at 55 degrees half of the bonds become accessible to glutathione. 5. From the results obtained with the proteins investigated, the conclusion reached is that the disulphide bonds of native proteins are structurally protected and do not react with glutathione under physiological conditions.
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PMID:The reactivity of the disulphide bonds of purified proteins in relationship to primary structure. 486 Apr 70

Components were solubilized from human glomerular basement membrane by digestion with collagenase and pepsin or by extraction with guanidine-HCl either directly or after previous digestion with the enzyme. The diverse preparations were used as antigens in the enzyme-linked immunosorbent assay (ELISA) of antibody titers in sera from patients with Goodpasture syndrome and patients with other forms of glomerulonephritis, that is, systemic lupus erythematosus, periarteritis nodosa, and IgA-related nephropathy. Patients with Goodpasture syndrome had high titers of IgG antibodies reacting most strongly with collagenase digests. The antigen(s) was only partly solubilized by guanidine-HCl extraction, was destroyed by pepsin digestion as well as reduction, and partly destroyed by trypsin digestion. The antigen(s) is most likely noncollagenous protein. Antibodies from patients with other forms of nephritis were directed primarily against antigens in guanidine-HCl extracts, while the antigen(s) was not solubilized by collagenase digestion. Pepsin digestion destroyed the antigen(s). The antibodies were of a different class, that is, the patients with systemic lupus erythematosus had IgG and IgA as well as IgM antibodies; the patients with periarteritis nodosa had IgM or IgG and IgA antibodies, while the patients with IgA-related nephritis had the highest recorded titers of IgA but also had IgG as well as IgM antibodies. None of the patients had antibodies directed against triple helical collagen. The antibody response in anti-GBM antibody-related nephritis, then, is different both with respect to antigen and antibody class and depends on the underlying disease syndrome.
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PMID:Antiglomerular basement membrane antibody: antibody specificity in different forms of glomerulonephritis. 613 25

The purpose of the study was to examine the effect of gamma irradiation on the enzymatic as well as the in vivo degradation of polyglycolic acid sutures. The sutures of size 2-0 were irradiated at dosage levels of 0-20 mrad. The three enzymes chosen for this study were esterase, alpha-chymotrypsin, and trypsin. The irradiated sutures were both immersed in the enzyme solutions; their corresponding buffer controls, and implanted in inbred black-and-white hooded hister rats (Liverpool strain). The degradation of PGA sutures was determined mechanically. Among the three enzymes studied, esterase showed the highest enzymatic effect on the degradation of the unirradiated and irradiated PGA sutures. Trypsin's effect on PGA sutures was not observed until 20 mrad. The findings of trypsin demonstrated the hypothesis that synthetic high molecular weight polymers, which are initially resistant to enzymatic degradation, could become prone to enzymatic attack after altering their physical and chemical structures. Implanted PGA sutures maintained a similar or slightly higher mean tensile breaking strength in in vivo degradation compared to in vitro degradation (0.1M tris buffer of pH = 7.5); these degradation profiles suggest that PGA does not display similar behavior in in vivo and in vitro degradations. The magnitude of dissimilarity depends on the radiation dosage and on the duration of degradation, and is speculated to be attributable to the specific action of enzymes with respect to the configuration and chemical structure of the PGA sutures.
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PMID:The effect of gamma irradiation on the enzymatic degradation of polyglycolic acid absorbable sutures. 631 94

To develop an animal model for acute carotid artery occlusion suitable for studying the retinal sequelae of this disease, we performed bilateral and unilateral common carotid artery ligations on mature pigmented rats. Bilateral ligation consistently resulted in a characteristic pathologic retinal appearance, paralleling the retinopathy of carotid artery occlusive disease in humans, demonstrated by fundus photography and fluorescein angiography. Any abnormalities found in the rats with unilateral ligations were inconsistent and less severe, although fluorescein angiography proved to be more sensitive than ophthalmoscopy for detecting these subtle changes. Pepsin-trypsin retinal digests disclosed extensive disruption of the microvasculature in the eyes of bilaterally ligated animals. This model should prove to be useful in examining the reversibility of the ocular findings as well as evaluating central nervous system abnormalities after carotid artery occlusion.
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PMID:An experimental model of carotid artery occlusive disease. 642 Nov 64

The possibility of preservation and restoration of antigenicity of some antigens in paraffin-embedded tissue was evaluated by direct immunofluorescent technique on deparaffinized sections. Fixation with 96% ethanol-1% acetic acid, 10% neutral buffered formalin and p-formaldehyde was useful for the preservation of tissue antigens and immune deposits, whose antigenicity could be easily restored by trypsin digestion. Neutral buffered formalin was also a satisfactory fixative in immunofluorescent staining on lymphocyte/plasma cell-bound immunoglobulins. Fixation with alcohol-Bouin's fluid showed contrast results; feasible for staining of cell-bound immunoglobulins, but poor for that of glomerular immune deposits. After papain digestion, BSA and lysozyme, antigens of immune complexes, were easily detected in experimental chronic serum sickness glomerulonephritis. Pepsin was more efficient than trypsin in restoring the antigenicity of renal tissue antigens such as fibronectin and polyantigenic basement membrane, but the brush border antigen of the proximal renal tubules was frail to the pepsin digestion. In general, the enzymatic digestion time necessary for the restoration of antigenicity was in parallel with fixation time. Results obtained have shown that deparaffinized sections could be used as satisfactory substrate for immunohistochemistry when proper fixation and efficient proteolytic enzymatic pretreatments were performed.
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PMID:Restoration of antigenicity of tissue antigens, cell-bound immunoglobulins and immune deposits in paraffin-embedded tissue. The influence of fixation and proteolytic enzymatic digestion. 643 48

The effect of several potentially harmful agents in gastric juice and duodenal contents on esophageal mucosa was investigated in the presence or absence of luminal H+ using an in vitro technique. Isolated rabbit esophageal mucosae were incubated in an Ussing chamber, and during exposure to the test agents mucosal integrity was assessed by measurement of mucosal potential difference (PD), tissue electrical resistance (R), and when luminal acid was present, the tissue permeability to H+. At pH 3.5 taurocholate caused a marked decrease in the PD and R and a substantial increase in the rate of luminal H+ loss. This effect was dependent on the presence of luminal H+, since no changes were observed with taurocholate at pH 7.4. In contrast, two of the three deconjugated bile salts tested at pH 7.4, deoxycholate and chenodeoxycholate, caused a profound reduction in the PD and R, similar to that observed with taurocholate in the presence of H+. Pepsin in the presence of H+, lysolecithin to a lesser degree, and trypsin in the absence of H+ also adversely affected isolated esophageal mucosa, but the effects were less pronounced than those caused by bile salts. Our data suggest that different mechanisms are operative in the pathogenesis of acidic and alkaline reflux esophagitis. In the presence of gastric H+, pepsin, and conjugated bile salts are the substances responsible for the greatest injury. In contrast, when acid is absent, trypsin and especially deconjugated bile salts are more crucial pathogenetic factors.
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PMID:Effect of bile salts and related compounds on isolated esophageal mucosa. 676 88

Human milk contains unsaturated lactoferrin and vitamin B12 binding protein. It has been suggested that these proteins may exert antibacterial effects in the intestine of the breast fed infant, but the effect of the intestinal environment on the antibacterial effect of these proteins has not been described. In this study human milk was treated with pepsin and trypsin and the influence of digestion on iron and vitamin B12 binding capacity, bacterial uptake of iron and vitamin B12 from milk and bacteriostatic effect was studied. Pepsin digestion had no effect on vitamin B12 binding capacity, or the ability of bacteria to take up vitamin B12, or the growth inhibitory effect on a vitamin B12 dependent strain. In contrast, trypsin digestion did not affect iron binding or bacteriostatic effects attributable to lactoferrin. The. findings support an in vivo bacteriostatic role for lactoferrin in the breast fed neonate's intestine but do not support a similar role for the vitamin B12 binding protein.
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PMID:The effect of digestive enzymes on the binding and bacteriostatic properties of lactoferrin and vitamin B12 binder in human milk. 677 68

Paraffin-embedded tissue can be used as substrate for immunohistochemistry after enzymatic treatment with proteases. The sensitivity of immunofluorescence on enzyme-treated paraffin sections and on unfixed cryostat sections is compared in this study. Pepsin was more efficient by weight than trypsin in restoring the antigenicity of immune deposits. Increased fluorescence intensity was obtained up to a pepsin concentration of 0.4%. Intensity was further increased when pepsin treated sections were treated with trypsin. Immune deposits were detected in enzyme treated, paraffin sections of kidneys of mice injected with anti-GBM diluted 1/200 or less and in cryostat sections of mice injected with anti-GBM diluted 1/400 or less. This small decrease in sensitivity is considered trivial compared with the advantage gained by the excellent preservation of the tissue.
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PMID:Detection of immune deposits in glomeruli: a comparative study of paraffin-embedded, enzyme-treated sections and cryostat sections as substrates in immunofluorescence. 677 25


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