Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.52 (PNGase F)
 1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Characteristic properties of the antigens recognized by sperm-immobilizing monoclonal antibodies (SI-mAbs) from different sources were compared by ELISA competitive inhibition assay, Western blot analysis, chromatographic analysis, and enzymatic digestion studies. Among 9 SI-mAbs, human mAb H6-3C4 and three mouse mAbs--2C6, 2B6, and 2E5--also possessed strong sperm-agglutinating activity. Binding of human mAb H6-3C4 to sperm was strongly inhibited by the three mouse mAbs (2C6, 2B6, and 2E5), but not by the rat or the other four mouse mAbs. SDS-PAGE revealed that mAb H6-3C4 and three mouse mAbs recognized the same antigen molecules of 15-25 kDa present in both sperm extracts and seminal plasma. Chemical treatments with trifluoromethanesulfonic acid and sodium metaperiodate destroyed the antigen determinants recognized by the above four mAbs, as detected by both ELISA and antibody absorption tests. Western blot analysis revealed that the antigens were susceptible to treatments with papain, proteinase K, and N-glycanase, but resistant to trypsin, V8 protease, and thermolysin. These results indicate that one of the major antigens recognized by mAbs with sperm-immobilizing action may be a sperm membrane-associated glycoprotein of 15-25 kDa and the epitope may involve N-linked oligosaccharides.
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PMID:Comparative studies of the antigens recognized by sperm-immobilizing monoclonal antibodies. 161 9

Two-dimensional gel electrophoresis (2DGE) and image processing were used to quantify protein and carbohydrate heterogeneity in human plasma fibronectin (FN) and its enzymatically produced domains. After a 30 minute thermolysin digest of FN, the domains were identified in 2DGE by their known isoelectric points and molecular weights, which were compared to domain standards purified by hydroxyapatite, gel exclusion and heparin-Sepharose chromatography. Three individual species were observed in the cell binding domain which may correspond to the heterogeneity known to result from alternative splicings of the fibronectin gene. In addition, the carbohydrate heterogeneity in the gelatin binding domain was analyzed by 2DGE and isoelectric focusing (IEF) before and after treatment with N-glycanase and neuraminidase to remove selected carbohydrate moieties. Five individual species which differ in carbohydrate structure were observed. The results also indicate a carbohydrate dependent stabilization of the gelatin binding domain with respect to proteolytic digestion.
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PMID:Separation and characterization of fibronectin domains by two-dimensional electrophoresis. 209 3