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)

Neuraminidase (Vibrio cholerae) treatment of human metastatic mammary carcinoma MDA-MB-231 cells grown in culture released 0.60-0.63 mg of N-acetylneuraminic acid from 10(9) cells. Incubation of intact cells with a modified trypsin and fractionation by gel filtration gave mainly O-glycopeptides. The presence of O-glycosyl-linked chains having one or two carbohydrate residues was confirmed by treatment of the glycopeptide fractions with galactose oxidase, followed by reduction with alkaline sodium borotritide and fractionation. The major glycopeptide fraction, which consisted of 53% carbohydrate and 47% protein, and a minor glycopeptide fraction each inhibited hemagglutination by peanut lectin. These results suggest the presence of O-beta-D-galactopyranosyl-(1 leads to 3)-O-(2-acetamido-2-deoxy-alpha-D-galactopyranosyl)-(1 leads to 3)-L-serine (threonine) residues. The absorptive capacities for anti-HLA-A2 and anti-HLA-B8 antisera were slightly greater for intact than for lyophilized cells, which suggested that masking of these major histocompatibility antigens did not occur in intact cells.
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PMID:Isolation and partial characterization of surface components of cell line MDA-MB-231 derived from a human metastatic breast carcinoma. 628 76

We have developed an experimental animal model to establish the patterns of sequestration of untreated, as well as chemically and enzymatically modified red blood cells (RBC). The intraperitoneal route of transfusion provides a useful way of transferring large numbers of untreated RBC into small animals and assuring their introduction into the circulation within 24 hr. Moreover, this route "filters" some types of modified erythrocytes, eg, glutaraldehyde treated RBC. From the pattern of sequestration, the RBC in the peritoneal cavity then pass through the liver where other types of modified RBC are sequestered, eg, after trypsin, pronase, protease, or sialidase treatment. Some modified RBC show a preference for the spleen as the site of sequestration, eg, galactose oxidase or N-ethylmaleimide treated RBC. These appear in the spleen despite intraperitoneal transfusion. Relevant to this study is the observation that in the rat old RBC are sequestered both by liver and spleen, while asialoerythrocytes are sequestered by liver only. A possible reason for this difference is discussed in the text.
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PMID:Studies on the sequestration of chemically and enzymatically modified erythrocytes. 631 Sep 89

Lucifer yellow CH, a fluorescent hydrazide, reacted with cell surface glycoconjugates on murine thymocytes oxidized with NaIO4 or galactose oxidase. Surface labeling was monitored by fluorescence microscopy, spectrophotometry and by flow microfluorometry. No labeling was detected in unoxidized cells and fluorescence was reduced by neuraminidase and by trypsin. Lucifer yellow CH derivatives of gangliosides also were prepared and incorporated into the surface membranes of thymocytes.
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PMID:Fluorescence labeling of cell surface glycoconjugates with Lucifer yellow CH. 684 85

Compared with croton oil- and thioglycolate-induced macrophages, the PHA-induced peritoneal macrophages showed th highest cytocidal activity against human malignant melanoma, mammary carcinoma and rat R3230 adenocarcinoma (AdCa) cells. Resident (physiological saline-induced) macrophages showed the lowest cytocidal activities. Vibrio cholera neuraminidase (VCN) and galactose oxidase increased, whereas trypsin, plasmin, papain and mild sonication decreased the cytotoxic function of macrophages against the neoplastic target cells. The effect of macrophage membrane prepartions on the cytocidal action of whole macrophages was also examined. VCN and galactose oxidase increased, whereas trypsin, plasmin, papain and mild sonication reduced the effects. It is concluded that the possible modulation of the cytocidal function of macrophages is due either to direct enzyme action on the macrophage surface, or to indirect enzyme action with enzymatically produced membrane preparations. Macrophage membrane preparations could either enhance or inhibit the antineoplastic action of the macrophags.
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PMID:Correlation between macrophages and their membrane fraction. Cytocidal activities on neoplastic cells. 699 9

Boar spermatozoa were radioactively labeled by either lactoperoxidase-catalysed iodination or galactose oxidase oxidation followed by reduction with tritiated sodium borohydride. Plasma membrane glycoproteins were solubilized with the non-ionic detergent Nonidet P40 and separated by affinity chromatography on concanavalin A-Sepharose. A major water-soluble concanavalin A receptor of molecular weight greater than 160 000 was isolated by gel filtration and ion-exchange chromatography. Its amino acid and carbohydrate composition were determined. This glycoprotein is susceptible to digestion by trypsin or chymotrypsin.
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PMID:The isolation and characterization of a concanavalin A receptor from boar spermatozoa surface. 723 91

Eight monoclonal antibodies (MAbs), designated RGM21 approximately RGM42, were generated against mucin purified from the rat gastric mucosa. By applying ELISA, all of these MAbs were proved to react not only with the purified mucin, but also with the oligosaccharide mixture obtained from the antigenic mucin by alkaline borohydride treatment. Treatment of the mucin-attached ELISA well with trypsin, sodium periodate or galactose oxidase prior to the addition of the MAb was applied to characterize these MAbs. Histochemical observation indicated that all these MAbs were able to stain the formalin fixed-paraffin embedded sections of the rat gastroduodenal mucosa. Although each of these MAbs reacted with distinct mucus-producing cells localized in particular regions of the gastroduodenal mucosa, their staining specificity could generally be classified into four groups. These MAbs might be useful for estimating the physiological and pathological changes of mucins in the gastric mucosa.
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PMID:Establishment of monoclonal antibodies against carbohydrate moiety of gastric mucins distributed in the different sites and layers of rat gastric mucosa. 891 13


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