PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8662763-13 1996 The complex between human alpha2M and plasma CPB dissociated during SDS-polyacrylamide gel electrophoresis and transverse urea gel electrophoresis suggesting that the interaction was noncovalent and depended on the tertiary structure of the native alpha2M molecule. Urea 122-126 alpha-2-macroglobulin Homo sapiens 26-33 17996290-5 2008 Differential scanning calorimetry and urea gel electrophoresis demonstrate that both bait region cleavage and covalent incorporation of protein ligands in the thioester pocket play critical roles in the stability of alpha2M complexes. Urea 38-42 alpha-2-macroglobulin Homo sapiens 216-223 8960406-7 1996 Serum- and alpha 2-macroglobulin-[125I]rh-inhibin complexes dissociated upon exposure to 8 M urea. Urea 93-97 alpha-2-macroglobulin Homo sapiens 11-32 1716880-0 1991 Kinetics of the urea-induced dissociation of human plasma alpha 2-macroglobulin as measured by small-angle neutron scattering. Urea 16-20 alpha-2-macroglobulin Homo sapiens 58-79 1375654-0 1992 Temperature dependence of the kinetics of the urea-induced dissociation of human plasma alpha 2-macroglobulin into half-molecules. Urea 46-50 alpha-2-macroglobulin Homo sapiens 88-109 1375654-2 1992 The kinetics of the urea-induced dissociation of human plasma alpha 2-macroglobulin to half-molecules has been studied as a function of temperature by using small-angle scattering of X-rays and neutrons. Urea 20-24 alpha-2-macroglobulin Homo sapiens 62-83 1716880-1 1991 The kinetics of the urea-induced dissociation of human plasma alpha 2-macroglobulin into two half-molecular fragments was investigated at 21.0 degrees C by using small-angle neutron scattering. Urea 20-24 alpha-2-macroglobulin Homo sapiens 62-83 1716880-9 1991 A structural analysis shows that the scattering curve of urea-dissociated alpha 2-macroglobulin can best be explained by that of a Gaussian coil with a radius of gyration equal to 9.44 nm. Urea 57-61 alpha-2-macroglobulin Homo sapiens 74-95 2447091-3 1988 Most of the 125I-TGF-beta.alpha 2M complex could be dissociated by acid or urea treatment. Urea 75-79 alpha-2-macroglobulin Homo sapiens 26-34 2462911-3 1988 Treatment of alpha 2M with either 0.5 mM dithiothreitol (DTT) or 4 M urea results in dissociation of the native tetramer into two half-molecules of Mr approximately 360,000. Urea 69-73 alpha-2-macroglobulin Homo sapiens 13-21 2462911-7 1988 High-performance size-exclusion chromatography and sedimentation velocity ultracentrifugation studies were then used to estimate the Stokes radius (Re) of alpha 2M and both DTT- and urea-induced half-molecules of alpha 2M. Urea 182-186 alpha-2-macroglobulin Homo sapiens 213-221 81204-4 1978 In the presence of 4 M urea, alpha2-macroglobulin dissociates into subunits and this dissociation does not lead to a release of the bound proteases. Urea 23-27 alpha-2-macroglobulin Homo sapiens 29-49 2445372-0 1987 Evidence for active half-molecules of alpha 2-macroglobulin formed by dissociation in urea. Urea 86-90 alpha-2-macroglobulin Homo sapiens 38-59 2445372-1 1987 Urea caused dissociation of alpha 2-macroglobulin (alpha 2M) into half-molecules (two disulfide-bonded subunits) as revealed by gel electrophoresis. Urea 0-4 alpha-2-macroglobulin Homo sapiens 28-49 2445372-1 1987 Urea caused dissociation of alpha 2-macroglobulin (alpha 2M) into half-molecules (two disulfide-bonded subunits) as revealed by gel electrophoresis. Urea 0-4 alpha-2-macroglobulin Homo sapiens 51-59 2445372-3 1987 Half-dissociation occurred at about 2.2 M. The ability of alpha 2M to inhibit trypsin also decreased with increasing urea concentration, but the activity-urea curve was shifted to the right as compared to the dissociation-urea curve. Urea 117-121 alpha-2-macroglobulin Homo sapiens 58-66 2445372-3 1987 Half-dissociation occurred at about 2.2 M. The ability of alpha 2M to inhibit trypsin also decreased with increasing urea concentration, but the activity-urea curve was shifted to the right as compared to the dissociation-urea curve. Urea 154-158 alpha-2-macroglobulin Homo sapiens 58-66 2445372-3 1987 Half-dissociation occurred at about 2.2 M. The ability of alpha 2M to inhibit trypsin also decreased with increasing urea concentration, but the activity-urea curve was shifted to the right as compared to the dissociation-urea curve. Urea 154-158 alpha-2-macroglobulin Homo sapiens 58-66 91367-15 1979 Exposure of S-alpha 2M to 3 M-urea or pH3 resulted in dissociation to the disulphide-bonded half-molecules; these did not show the proteinase-binding activity characteristic of the intact alpha 2M. Urea 30-34 alpha-2-macroglobulin Homo sapiens 14-22 90334-2 1979 coli L-asparaginase by alpha 2-macroglobulin (alpha 2M) was observed under conditions otherwise propitious to the dissociation of the tetrameric molecule into inactive subunits, i.e. very diluted enzyme solutions or the presence of either SDS or urea. Urea 246-250 alpha-2-macroglobulin Homo sapiens 23-44 90334-2 1979 coli L-asparaginase by alpha 2-macroglobulin (alpha 2M) was observed under conditions otherwise propitious to the dissociation of the tetrameric molecule into inactive subunits, i.e. very diluted enzyme solutions or the presence of either SDS or urea. Urea 246-250 alpha-2-macroglobulin Homo sapiens 46-54 80217-2 1978 As well as having no detectable impurities by the usual criteria for testing the homogeneity of protein preparations, these alpha2M preparations showed a single component, after reduction in urea, of 185000 daltons by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Urea 191-195 alpha-2-macroglobulin Homo sapiens 124-131 80217-6 1978 The cleavage of the 185000-dalton subunit to a 85000-dalton species on interaction of trypsin with alpha2M was demonstrated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis after reduction of the alpha2M-trypsin complex in urea. Urea 236-240 alpha-2-macroglobulin Homo sapiens 99-106 80217-6 1978 The cleavage of the 185000-dalton subunit to a 85000-dalton species on interaction of trypsin with alpha2M was demonstrated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis after reduction of the alpha2M-trypsin complex in urea. Urea 236-240 alpha-2-macroglobulin Homo sapiens 209-216 13737545-0 1960 The use of urea-starch-gel electrophoresis in studies of reductive cleavage of an alpha 2-macroglobulin. Urea 11-15 alpha-2-macroglobulin Homo sapiens 82-103