PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12353073-3 2002 The variant forms SDS-stable complexes with activated factor X (fXa) and its thermal stability and rate of factor Xa inhibition in the absence of heparin are identical to those of normal antithrombin. Sodium Dodecyl Sulfate 18-21 serpin family C member 1 Homo sapiens 187-199 11551226-8 2001 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate 32-35 serpin family C member 1 Homo sapiens 56-72 11551226-8 2001 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate 32-35 serpin family C member 1 Homo sapiens 74-79 11551226-8 2001 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate 32-35 serpin family C member 1 Homo sapiens 151-156 11551226-8 2001 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate 32-35 serpin family C member 1 Homo sapiens 151-156 8619306-4 1995 alpha 2-Antiplasmin, proteinase alpha 1-inhibitor, antithrombin III and ITI with collagen yield complexes that are resistant to urea, sodium dodecylsulfate, and Trilon B. Sodium Dodecyl Sulfate 134-155 serpin family C member 1 Homo sapiens 21-67 9794814-5 1998 An antithrombin to papain inactivation stoichiometry of approximately 3 indicated extensive cleavage of the inhibitor concurrent with enzyme inactivation, a behaviour verified by SDS/PAGE. Sodium Dodecyl Sulfate 179-182 serpin family C member 1 Homo sapiens 3-15 9794814-7 1998 The papain band in SDS/PAGE progressively disappeared on reaction of the enzyme with increasing amounts of antithrombin, but no band representing a stable antithrombin-papain complex appeared. Sodium Dodecyl Sulfate 19-22 serpin family C member 1 Homo sapiens 107-119 7606009-3 1995 Iodine at levels of 0.01% to 0.02% caused between 43% and 94% loss of AT-III activity, as well as degradation of AT-III as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis. Sodium Dodecyl Sulfate 132-154 serpin family C member 1 Homo sapiens 113-119 7647008-1 1995 The M(r) of the complexes formed when factor Xa reacts with antithrombin III (ATIII) in plasma were estimated by gel filtration and SDS-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 132-135 serpin family C member 1 Homo sapiens 60-76 7647008-1 1995 The M(r) of the complexes formed when factor Xa reacts with antithrombin III (ATIII) in plasma were estimated by gel filtration and SDS-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 132-135 serpin family C member 1 Homo sapiens 78-83 7730349-4 1995 AT-Denver inhibited thrombin and Factor Xa with nearly equimolar stoichiometries and formed SDS-stable complexes with these proteinases, indicating that the diminished inhibitor activity was not due to an enhanced turnover of the inhibitor as a substrate. Sodium Dodecyl Sulfate 92-95 serpin family C member 1 Homo sapiens 0-2 7692967-5 1993 Consistent with these results, SDS gel electrophoresis of the 125I-labeled kallikrein-inhibitor complexes formed in a mixture of these kallikrein inhibitors at their relative plasma concentrations indicated that antithrombin effectively competed with C1-inhibitor and alpha 2-macroglobulin for kallikrein, accounting for 54% of the total kallikrein complexes, only when both heparin and H-kininogen were present. Sodium Dodecyl Sulfate 31-34 serpin family C member 1 Homo sapiens 212-224 7863481-4 1994 The effect of a denaturing agent (sodium dodecyl sulfate) on the recognition of the plasma antithrombin by a polyclonal antibody was studied in an immuno-enzymatic assay. Sodium Dodecyl Sulfate 34-56 serpin family C member 1 Homo sapiens 91-103 8419351-6 1993 A 1:1 stoichiometric complex between factor VIIa and antithrombin III, with an apparent molecular weight of 110,000, was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 133-155 serpin family C member 1 Homo sapiens 44-69 1911389-5 1991 On sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), prior to its application to thrombin-Sepharose, the antithrombin migrated as a single band with identical mobility to that of normal antithrombin. Sodium Dodecyl Sulfate 3-26 serpin family C member 1 Homo sapiens 126-138 1440655-6 1992 In SDS-PAGE inactivation of human antithrombin III was correlated with the occurrence of two cleavage products. Sodium Dodecyl Sulfate 3-6 serpin family C member 1 Homo sapiens 34-50 1519763-0 1992 Enzyme-linked immunosorbent assay for proteolytically inactivated antithrombin-III: use of sodium dodecyl sulfate to eliminate signal due to intact antithrombin-III. Sodium Dodecyl Sulfate 91-113 serpin family C member 1 Homo sapiens 66-82 1519763-4 1992 Using sodium dodecyl sulfate (SDS), we were able to devise an enzyme-linked immunosorbent assay (ELISA) capable of detecting cleaved AT-III in the presence of intact AT-III. Sodium Dodecyl Sulfate 6-28 serpin family C member 1 Homo sapiens 133-139 1519763-4 1992 Using sodium dodecyl sulfate (SDS), we were able to devise an enzyme-linked immunosorbent assay (ELISA) capable of detecting cleaved AT-III in the presence of intact AT-III. Sodium Dodecyl Sulfate 30-33 serpin family C member 1 Homo sapiens 133-139 1519763-4 1992 Using sodium dodecyl sulfate (SDS), we were able to devise an enzyme-linked immunosorbent assay (ELISA) capable of detecting cleaved AT-III in the presence of intact AT-III. Sodium Dodecyl Sulfate 30-33 serpin family C member 1 Homo sapiens 166-172 1519763-5 1992 It seems likely that the SDS alters the intact AT-III so that it is not detected in the ELISA. Sodium Dodecyl Sulfate 25-28 serpin family C member 1 Homo sapiens 47-53 1911389-5 1991 On sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), prior to its application to thrombin-Sepharose, the antithrombin migrated as a single band with identical mobility to that of normal antithrombin. Sodium Dodecyl Sulfate 63-66 serpin family C member 1 Homo sapiens 126-138 2029579-4 1991 When AT-III was isolated from the plasma of the propositus by heparin-Sepharose chromatography, it had identical mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to normal plasma-derived AT-III, under both reducing and nonreducing conditions. Sodium Dodecyl Sulfate 125-147 serpin family C member 1 Homo sapiens 5-11 2029579-4 1991 When AT-III was isolated from the plasma of the propositus by heparin-Sepharose chromatography, it had identical mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to normal plasma-derived AT-III, under both reducing and nonreducing conditions. Sodium Dodecyl Sulfate 184-187 serpin family C member 1 Homo sapiens 5-11 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sodium Dodecyl Sulfate 196-199 serpin family C member 1 Homo sapiens 13-19 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sodium Dodecyl Sulfate 196-199 serpin family C member 1 Homo sapiens 76-82 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sodium Dodecyl Sulfate 196-199 serpin family C member 1 Homo sapiens 76-82 2207328-4 1990 Immunoprecipitation of the cell-free translation mixture with rabbit polyclonal antibodies to AT-III showed, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), a 47-Kd polypeptide which is the non-glycosylated mature form of plasma AT-III. Sodium Dodecyl Sulfate 112-134 serpin family C member 1 Homo sapiens 94-100 2207328-4 1990 Immunoprecipitation of the cell-free translation mixture with rabbit polyclonal antibodies to AT-III showed, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), a 47-Kd polypeptide which is the non-glycosylated mature form of plasma AT-III. Sodium Dodecyl Sulfate 171-174 serpin family C member 1 Homo sapiens 94-100 2363123-9 1990 The abnormal AT III showed a normal antiprotease activity, a normal molecular weight by SDS-PAGE, but displayed only a partial immunological identity with the normal protein. Sodium Dodecyl Sulfate 88-91 serpin family C member 1 Homo sapiens 13-19 2154059-6 1990 In SDS-polyacrylamide gel electrophoresis and immunoblotting analysis, we found a complex formation of ATIII with both human and rabbit TM (and further confirmed their presence with isoelectrofocusing electrophoresis- data not shown). Sodium Dodecyl Sulfate 3-6 serpin family C member 1 Homo sapiens 103-108 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 267-289 serpin family C member 1 Homo sapiens 40-45 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 267-289 serpin family C member 1 Homo sapiens 134-139 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 291-294 serpin family C member 1 Homo sapiens 40-45 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 291-294 serpin family C member 1 Homo sapiens 134-139 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 291-294 serpin family C member 1 Homo sapiens 134-139 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 267-289 serpin family C member 1 Homo sapiens 134-139 3606566-8 1987 Owing to the association of S protein with the thrombin-antithrombin III (TAT) complex, the STAT complex assembled in vitro exhibited a higher Mr than the TAT complex as judged by polyacrylamide-gradient-gel electrophoresis in the absence of SDS. Sodium Dodecyl Sulfate 242-245 serpin family C member 1 Homo sapiens 56-72 3663509-5 1987 The AT III had a reduced ability to inactivate thrombin, when this was monitored by substrate hydrolysis or by SDS polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 111-114 serpin family C member 1 Homo sapiens 4-10 3187951-9 1988 SDS-PAGE experiments performed in purified system and immunoblots obtained from plasma showed that the two variants have different behaviour: in the case of AT III Charleville thrombin induced an apparent 5 k delta increase in molecular mass, probably due to a conformational change. Sodium Dodecyl Sulfate 0-3 serpin family C member 1 Homo sapiens 157-163 3801671-9 1987 Interaction of thrombin Tokushima with antithrombin III was much slower than "thrombin" when followed by SDS-PAGE. Sodium Dodecyl Sulfate 105-108 serpin family C member 1 Homo sapiens 39-55 3526065-1 1986 Urinary antithrombin III (AT III) related antigen was analyzed by SDS-polyacrylamide gel electrophoresis and Western blotting, and the nitrocellulose membrane was scanned with a 2-wavelength TLC scanner. Sodium Dodecyl Sulfate 66-69 serpin family C member 1 Homo sapiens 26-32 7426659-11 1980 Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis. Sodium Dodecyl Sulfate 0-22 serpin family C member 1 Homo sapiens 71-87 3699029-7 1986 The fast formation of the covalent complex between thrombin and antithrombin III in the presence of heparin was impaired as a result of the presence of S protein, as was shown by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Sodium Dodecyl Sulfate 233-255 serpin family C member 1 Homo sapiens 64-80 3486013-5 1986 These results were confirmed in a qualitative manner by directly monitoring the generation of factor XIa-antithrombin interaction product with sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis using an antibody population specific for the protease inhibitor. Sodium Dodecyl Sulfate 201-204 serpin family C member 1 Homo sapiens 105-117 3512602-5 1986 When thrombin-antithrombin (TAT) complexes were formed by incubating with excess thrombin, SDS-polyacrylamide gel electrophoresis (PAGE) analysis revealed that half the patient AT-III formed TAT complexes while the remainder migrated as free AT-III. Sodium Dodecyl Sulfate 91-94 serpin family C member 1 Homo sapiens 14-26 3512602-7 1986 The patient"s nonreacting AT-III (AT-III "Denver"), isolated by affinity chromatography, showed CIE and SDS-PAGE migration patterns characteristic of normal AT-III but failed to bind thrombin or Xa. Sodium Dodecyl Sulfate 104-107 serpin family C member 1 Homo sapiens 26-32 3512602-7 1986 The patient"s nonreacting AT-III (AT-III "Denver"), isolated by affinity chromatography, showed CIE and SDS-PAGE migration patterns characteristic of normal AT-III but failed to bind thrombin or Xa. Sodium Dodecyl Sulfate 104-107 serpin family C member 1 Homo sapiens 34-40 3512602-7 1986 The patient"s nonreacting AT-III (AT-III "Denver"), isolated by affinity chromatography, showed CIE and SDS-PAGE migration patterns characteristic of normal AT-III but failed to bind thrombin or Xa. Sodium Dodecyl Sulfate 104-107 serpin family C member 1 Homo sapiens 34-40 2415521-4 1985 Upon prolonged boiling in SDS it dissociates into 56- and 32-kDa components which co-migrate in SDS-PAGE with purified antithrombin III and thrombin, respectively. Sodium Dodecyl Sulfate 26-29 serpin family C member 1 Homo sapiens 119-135 6546700-10 1984 Interaction with antithrombin III is slower than normal when followed by SDS gel electrophoresis and inhibition of the amidolytic activity of thrombin on S2238. Sodium Dodecyl Sulfate 73-76 serpin family C member 1 Homo sapiens 17-33 7037067-2 1982 Proteolysis of residual AT-III was assessed on the basis of distribution of radioactivity in SDS-polyacrylamide gels after electrophoresis. Sodium Dodecyl Sulfate 93-96 serpin family C member 1 Homo sapiens 24-30 7426659-11 1980 Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis. Sodium Dodecyl Sulfate 0-22 serpin family C member 1 Homo sapiens 145-161 7426659-11 1980 Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis. Sodium Dodecyl Sulfate 24-27 serpin family C member 1 Homo sapiens 71-87 7426659-11 1980 Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis. Sodium Dodecyl Sulfate 24-27 serpin family C member 1 Homo sapiens 145-161 7213342-4 1980 Discontinuous polyacrylamide-gel electrophoresis of the reduced dissociation fragments of the complex in the presence of sodium dodecyl sulphate reveals two antithrombin III bands that do not resolve during electrophoresis without reduction. Sodium Dodecyl Sulfate 121-144 serpin family C member 1 Homo sapiens 157-173 1194266-7 1975 The addition of heparin dramatically accelerates the rate of this interaction with virtually complete inhibition of Factor IXa occurring within 15 s. Sodium dodecyl sulfate gel electrophoresis of reduced and nonreduced proteins indicates that antithrombin-heparin cofactor functions as a potent inhibitor of Factor IXa by forming an undissociable complex with the enzyme which is stable in the presence of denaturing or reducing agents (or both). Sodium Dodecyl Sulfate 150-172 serpin family C member 1 Homo sapiens 243-255 316999-7 1979 The molecular weight estimated on SDS electrophoresis for AT-III and alpha 1-AT was 63,000 and 50,000, respectively. Sodium Dodecyl Sulfate 34-37 serpin family C member 1 Homo sapiens 58-64 420768-4 1979 The enzyme--antithrombin complexes could not be dissociated with sodium dodecyl sulfate (NaDodSO4) but the NaDodSO4-denatured complexes were dissociated by hydroxylamine treatment. Sodium Dodecyl Sulfate 65-87 serpin family C member 1 Homo sapiens 12-24 65284-2 1977 The labelled antithrombin III has a high specific activity (5.75 units/mg) and displayed a single band on SDS-polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 106-109 serpin family C member 1 Homo sapiens 13-29 20211924-6 2011 Antithrombin"s ability to form sodium dodecyl sulfate (SDS)-stable complex with thrombin, stoichiometry of thrombin inhibition, second-order rate constant for thrombin and factor Xa (fXa) inhibition (M(-1) s(-1)), and heparin dissociation constant (K(D); tryptophan fluorescence emission spectra) were determined. Sodium Dodecyl Sulfate 31-53 serpin family C member 1 Homo sapiens 0-12 21297450-1 2011 The effect of protamine sulfate on factor Xa (FXa) and the factor Xa-antithrombin complex was studied via SDS-PAGE and Western blot analysis. Sodium Dodecyl Sulfate 106-109 serpin family C member 1 Homo sapiens 69-81 20211924-6 2011 Antithrombin"s ability to form sodium dodecyl sulfate (SDS)-stable complex with thrombin, stoichiometry of thrombin inhibition, second-order rate constant for thrombin and factor Xa (fXa) inhibition (M(-1) s(-1)), and heparin dissociation constant (K(D); tryptophan fluorescence emission spectra) were determined. Sodium Dodecyl Sulfate 55-58 serpin family C member 1 Homo sapiens 0-12 17879089-0 2007 Comparison of planar SDS-PAGE, CGE-on-a-chip, and MALDI-TOF mass spectrometry for analysis of the enzymatic de-N-glycosylation of antithrombin III and coagulation factor IX with PNGase F. Three different analytical techniques (planar SDS-PAGE, CGE-on-a-chip and MALDI-TOF-MS) applied for determination of the molecular weight of intact and partly and completely de-N-glycosylated human serum glycoproteins (antithrombin III and coagulation factor IX) have been compared. Sodium Dodecyl Sulfate 234-237 serpin family C member 1 Homo sapiens 130-146 17584894-6 2007 SDS-PAGE showed that OTR4120 induced the formation of covalently linked complexes between antithrombin III or heparin cofactor II and thrombin. Sodium Dodecyl Sulfate 0-3 serpin family C member 1 Homo sapiens 90-106 15664348-4 2005 The purity of the AT III from this one-step purification is 93% as measured by SDS-PAGE and the protein recovery yield is about 90%. Sodium Dodecyl Sulfate 79-82 serpin family C member 1 Homo sapiens 18-24 12907439-3 2003 Antithrombin Cambridge II was found to be normal in its affinity for heparin, its ability to form sodium dodecyl sulfate-stable complexes with factor Xa and thrombin, and its uncatalyzed stoichiometries and rates of inhibition. Sodium Dodecyl Sulfate 98-120 serpin family C member 1 Homo sapiens 0-12 14532267-3 2003 All chimeras bound heparin with a high affinity similar to wild-type, underwent heparin-induced fluorescence changes indicative of normal conformational activation, and were able to form SDS-stable complexes with thrombin, factor Xa, and factor IXa and inhibit these proteases with stoichiometries minimally altered from those of wild-type antithrombin. Sodium Dodecyl Sulfate 187-190 serpin family C member 1 Homo sapiens 340-352