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)

Ovarian carcinoma contains an antigen (TA) which is stable at 100 degrees. Rabbit antisera to glycoprotein-rich extracts of tumors detect TA in 70 per cent of ovarian malignancies, in some benign ovarian cysts, certain normal lung preparations, normal cervix, and squamous-cell carcinoma of the cervix. Highest levels may be associated with mucin secretion. No detectible antigen was present in normal ovary, plasma, A, B, and O erythrocytes, leukocytes, placenta, brain, heart, liver, corpus uteri, spleen, skeletal muscle, or kidney. Prolonged digestion of boiled tumor extracts with papain, trypsin, chymotrypsin, on Sephadex G-150 corresponding to a globular protein of 27,000 to 36,000 molecular weight. A beta-globulin mobility is seen in immunoelectrophoresis. It appears that TA differs in tissue specificity and molecular size from other known ovarian cancer associated antigens.
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PMID:A thermostable antigen associated with ovarian cancer. 6 15

Bovine erythrocyte treatment with chymotrypsin, trypsin, pronase, papain, or ficin eliminated or weakened the reactivity of 18 of the 47 blood group factors which were examined. Thirteen of the affected factors were from the B system, and one each was from the C, FV, L, M, and R'S' systems. Variation attributable to pheno-group (allele) or genotype influences was observed in the effects upon six of the factors. Ficin-treated V/V, but not F/V or F/F, cells were rapidly lysed by normal rabbit serum (complement control). Absorptions with pronase-treated V positive cells indicated that essentially all V antigenicity was removed. However, immunizations with pronase-treated V positive cells elicited V antibody production in one of two recipient cows. The numbers of antigens removed by different enzymes did not appear to be closely related to the amount of protein removed.
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PMID:Removal of blood group determinants from bovine erythrocyte membranes. 3. Action of proteolytic enzymes on intact cells. 6 56

The neoantigenic determinants (neoAg) which have been identified in the human C5b-9 membranolytic C complex were detected here by the direct fluorescent antibody technique on the surface of 27 +/- 11% of viable peripheral blood leukocytes (PBL). The cells were prepared from defibrinated blood by sedimentation on Ficoll-Hypaque. Specificity of the antisera was established by quantitative inhibition of the fluorescent staining reaction, and of agglutination of EAC1-7, by highly purified C5b-9 complex. No inhibition was observed with fresh normal human serum. The majority of the PBL with surface neoAg was found in the B lymphocyte subpopulation that failed to form rosettes with sheep erythrocytes. NeoAg on B lymphocytes was removed to differing degrees by trypsin, papain, or pepsin treatment, and by maintaining the cells at 4 degree C for 20 hr in serum-free medium. The individual components, C5, C6, C7, C8, and C9, were also detected on the surface of PBL. With differential fluorescent stains, C5 and neoAg as well as C8 and neoAg could be detected on the same cells. The results indicate that viable B lymphocytes prepared from defibrinated blood, have the components of the membrane attack complex of C on their surface. The concomitant occurrence of the neoAg indicates that these proteins are present at least in part in the form of the assembled terminal complex.
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PMID:Leukocyte complement: neoantigens of the membrane attack complex on the surface of human leukocytes prepared from defibrinated blood. 7 29

A simple method using a cationic dye, toluidine blue (TB), to quantify changes of red cell membrane area has been developed and tested for its validity. After incubating a glucose-depleted red cell suspension with a fixed quantity of TB at 37 degrees C for 10 min, the remaining TB was measured spectrophotometrically at 640 nm. Using this technique, we were able to show differences in TB uptake by populations of young and old red cells. The exact mechanism for TB uptake by the red cells is not clear. Treatment of the cells with bromelin, papain and trypsin reduced the uptake of TB, but neuraminidase and ficin had little or no effect. No inhibition of TB removal by red cells was observed using heparin, D-glucose, glucuronic acid, or N-acetylglucosamine.
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PMID:Evaluation of toluidine blue for measuring erythrocyte membrane loss during in vivo ageing. 8 Oct 69

Authors studied the occurrence of antibodies agglutinating IgG determinants with Rh positive red blood cells covered with IgG molecules of anti-Rh(D) activity treated with papain, pepsin, and trypsin. The occurrence of Fab antibodies was studied in the sera of newborn and of 1-6 years old healthy children, further on quantitative immunoglobulin assays were performed in these to determine whether homoreactant antibodies influence IgG production. Based on their results authors conclude that homoreactant antibodies do not influence IgG production. Authors assume a role in the IgG catabolism viz., they are involved in the elimination of antigen-antibody complexes.
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PMID:The occurrence of homoreactant factors and the examination of their influence on IgG synthesis. 8 27

Studies in physicochemical and immunochemical properties of polipeptide chains fragments of immunoglobulin G malignant growth permitted detecting the location site for a specific determinant which adds a unique feature to the whole molecule of immunoglobulin G. The specific antigenic determinant is defined by a group of amino acids located in the heavy chain site corresponding to Fd-fragment. During papain and trypsin hydrolysis of specific immunoglobulin G obtained from different patients the formed sets of fragments and peptides are different. This testifies to the fact that the immunoglobulin under study may belong to any of four subclasses of immunoglobulin G, that is confirmed by the immunochemical analysis with application of monospecific antisera against certain subclasses of immunoglobulin G.
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PMID:[Physicochemical and immunochemical properties of submolecular structures of immunoglobulin G characteristic of cancer]. 8 21

Plasma membranes were isolated from the leukemia cell line ASL1w and extracted with detergent (DOC). DOC solubilized more TL activity than could be detected on isolated membranes. However, extraction of membranes with LDS or EDTA solubilized only 17% and 4%, respectively, of the activity. This indicated that TL was not loosely associated with the membrane but rather was integrated into the lipid bilayer. At low concentrations of DOC (0.05%), TL was found to be largely aggregated and was also prone to autolysis. Neither aggregation nor autolysis was observed at a higher DOC concentration (0.5%). The apparent molecular weight of TL in 0.5% DOC was determined by Sephadex G-200 chromatography to be about 65,000-70,000. Digestion of a 0.5% DOC extract of TL with either papain or trypsin produced a fragment of TL of about 35,000 molecular weight. These fragments were similar in size to a fragment produced by autolysis. These data suggested that a region of the TL molecule was very prone to proteolytic attack. The 35,000 molecular weight proteolytic fragments bound specifically to lentil lectin affinity columns, which indicated that they retained at least part of the carbohydrate present on the native molecule.
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PMID:Some structural properties of thymus leukemia antigen (TL) solubilized with detergent. 9 17

The Rho(D) antigen of red cell membranes was solubilized using ethylene-diamine tetraacetic acid (EDTA) and 2-mercaptoethanol. The solubilized antigen was partially separated from other solubilized membrane components using molecular filtration. The antigen was treated with various enzymes to learn some of the chemical characteristics. It was found that the activity of the antigen, as measured by hemagglutination inhibition, was not affected by bee venom phospholipase A, Clostridium welchii phospholipase C, calf-intestinal alkaline phosphatase, Vibrio cholerae neuraminidase, pig kidney leucine aminopeptidase, bovine pancreatic carboxypeptidase A, and pig pancreatic carboxypeptidase B. However, the proteolytic enzymes, pronase, trypsin, chymotrypsin and papain, did destroy Rho(D) activity as measured by hemagglutination inhibition. These results indicate that protein is an important part of the active determinant of the Rho(D) antigen. The experiments by other investigators have shown that lipid is important to maintain the Rho(D) activity in the intact membrane; lipid probably helps to maintain the structural conformation of the Rho(D) molecule in its natural environment. The solubilized Rho(D) molecules are apparently not dependent on lipid for their Rho(D) activity.
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PMID:Studies on the characterization of the Rho(D) antigen. 10 79

Limited proteolysis of myosin by such proteolytic enzymes as trypsin, chymotrypsin or papain produces typical fragmentation of its heavy chain. Presently evidence is given that trypsin treatment cleaves the alkali light chain A-1 (20,700 dalton) to a shorter (ca 20,000 dalton) chain. The two "essential" thiols (SH-1 and 2) of moysin were alkylated with 17-C-N-ethylmaleimide and a non-negligible amount of radioactivity was also found in the two alkali light chains. Using the specific radioactivity of alkali light chain A-1 it was possible to identify it among heavy chain fragmentation products. The molecular weight of the newly formed A-1 indicates that limited tryptic cleavage of this A-1 confers on it a closer similarity with alkali light chain A-2.
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PMID:[Fragmentation of myosin A-1 light chain of fast muscle by trypsin]. 11 21

The biochemical nature of the neuraminidase-sensitive Mycoplasma pneumoniae receptor site on human lung fibroblast cells was studied. Purified, mixed sialoglycolipid (ganglioside) preparations from human and bovine tissues did not bind to M. pneumoniae organisms and block their subsequent attachment to fibroblasts. Fibroblasts incubated for 24 h in sialoglycolipid solutions to increase the ganglioside content of their membranes did not show increased pathogen attachment when later incubated with mycoplasmas. HeLa cells grown in the presence of sodium butyrate to increase GM3 ganglioside levels likewise did not have significantly increased uptake of M. pneumoniae organisms. Treatment of fibroblasts with enzymes indicated that the mycoplasma receptor site is trypsin and papain resistant but Pronase sensitive. Pronase digests of fibroblast membranes contained a product(s) which combined with M. pneumoniae cellls and cosedimented with them during centrifugation. Glycoproteins, purified from fibroblast membranes by a lithium diiodosalicylate solubilization technique, similarly bound to M. pneumoniae organisms. Collectively, these data suggest that the major component of the M. pneumoniae receptor site is a sialoglycoprotein with little or no lipid.
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PMID:Interaction of Mycoplasma pneumoniae with human lung fibroblasts: role of receptor sites. 11 49


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