The Experts below are selected from a list of 12 Experts worldwide ranked by ideXlab platform
Guido Tans - One of the best experts on this subject based on the ideXlab platform.
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Purification and Characterization of Multisquamase, the Prothrombin Activator Present in Echis Multisquamatus Venom
Thrombosis Research, 1997Co-Authors: Ramona J Petrovan, Götz Nowak, José W. P. Govers-riemslag, Jan Rosing, H. Coenraad Hemker, Guido TansAbstract:Abstract The venom of Echis multisquamatus (Central Asian sand viper) contains a single prothrombin activator, designated multisquamase, which is structurally and functionally different from ecarin, the prothrombin activator from the venom of Echis carinatus (saw-scaled viper). Multisquamase is comprised of a 58000 Mr and a 23000 Mr subunit that consists of two disulfide-linked chains of 12000 Mr and 10000 Mr, respectively. In contrast to ecarin, which activates prothrombin and prethrombin 1 at comparable rates, and whose activity is hardly affected by Ca2+ or by changes in ionic strength, multisquamase hardly activates prethrombin 1; prothrombin activation requires Ca2+ and is strongly inhibited at high ionic strength. The most favourable kinetic parameters are observed at 1 mM Ca2+ and at low ionic strength (Km = 0.085 μM and kcat = 0.68 s−1 at I ≅ 0.04). An increase in ionic strength considerably reduces the rate of prothrombin activation, due to an increase of the Km (Km = 0.8 μM and kcat = 1.03 s−1 at I ≅ 0.2). Studies in plasmas from patients on oral anticoagulant therapy show that E. Multisquamatus venom only activates carboxylated prothrombin, whereas E. carinatus activates both prothrombin and descarboxyprothrombin. Thus, multisquamase-dependent prothrombin activation appears to require post-translational modification of the gla-domain. This venom prothrombin activator may, therefore, become a useful tool to quantitate prothrombin and descarboxyprothrombin in cases where vitamin K-dependent carboxylation of prothrombin is impaired.
Ramona J Petrovan - One of the best experts on this subject based on the ideXlab platform.
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Purification and Characterization of Multisquamase, the Prothrombin Activator Present in Echis Multisquamatus Venom
Thrombosis Research, 1997Co-Authors: Ramona J Petrovan, Götz Nowak, José W. P. Govers-riemslag, Jan Rosing, H. Coenraad Hemker, Guido TansAbstract:Abstract The venom of Echis multisquamatus (Central Asian sand viper) contains a single prothrombin activator, designated multisquamase, which is structurally and functionally different from ecarin, the prothrombin activator from the venom of Echis carinatus (saw-scaled viper). Multisquamase is comprised of a 58000 Mr and a 23000 Mr subunit that consists of two disulfide-linked chains of 12000 Mr and 10000 Mr, respectively. In contrast to ecarin, which activates prothrombin and prethrombin 1 at comparable rates, and whose activity is hardly affected by Ca2+ or by changes in ionic strength, multisquamase hardly activates prethrombin 1; prothrombin activation requires Ca2+ and is strongly inhibited at high ionic strength. The most favourable kinetic parameters are observed at 1 mM Ca2+ and at low ionic strength (Km = 0.085 μM and kcat = 0.68 s−1 at I ≅ 0.04). An increase in ionic strength considerably reduces the rate of prothrombin activation, due to an increase of the Km (Km = 0.8 μM and kcat = 1.03 s−1 at I ≅ 0.2). Studies in plasmas from patients on oral anticoagulant therapy show that E. Multisquamatus venom only activates carboxylated prothrombin, whereas E. carinatus activates both prothrombin and descarboxyprothrombin. Thus, multisquamase-dependent prothrombin activation appears to require post-translational modification of the gla-domain. This venom prothrombin activator may, therefore, become a useful tool to quantitate prothrombin and descarboxyprothrombin in cases where vitamin K-dependent carboxylation of prothrombin is impaired.
Götz Nowak - One of the best experts on this subject based on the ideXlab platform.
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Purification and Characterization of Multisquamase, the Prothrombin Activator Present in Echis Multisquamatus Venom
Thrombosis Research, 1997Co-Authors: Ramona J Petrovan, Götz Nowak, José W. P. Govers-riemslag, Jan Rosing, H. Coenraad Hemker, Guido TansAbstract:Abstract The venom of Echis multisquamatus (Central Asian sand viper) contains a single prothrombin activator, designated multisquamase, which is structurally and functionally different from ecarin, the prothrombin activator from the venom of Echis carinatus (saw-scaled viper). Multisquamase is comprised of a 58000 Mr and a 23000 Mr subunit that consists of two disulfide-linked chains of 12000 Mr and 10000 Mr, respectively. In contrast to ecarin, which activates prothrombin and prethrombin 1 at comparable rates, and whose activity is hardly affected by Ca2+ or by changes in ionic strength, multisquamase hardly activates prethrombin 1; prothrombin activation requires Ca2+ and is strongly inhibited at high ionic strength. The most favourable kinetic parameters are observed at 1 mM Ca2+ and at low ionic strength (Km = 0.085 μM and kcat = 0.68 s−1 at I ≅ 0.04). An increase in ionic strength considerably reduces the rate of prothrombin activation, due to an increase of the Km (Km = 0.8 μM and kcat = 1.03 s−1 at I ≅ 0.2). Studies in plasmas from patients on oral anticoagulant therapy show that E. Multisquamatus venom only activates carboxylated prothrombin, whereas E. carinatus activates both prothrombin and descarboxyprothrombin. Thus, multisquamase-dependent prothrombin activation appears to require post-translational modification of the gla-domain. This venom prothrombin activator may, therefore, become a useful tool to quantitate prothrombin and descarboxyprothrombin in cases where vitamin K-dependent carboxylation of prothrombin is impaired.
José W. P. Govers-riemslag - One of the best experts on this subject based on the ideXlab platform.
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Purification and Characterization of Multisquamase, the Prothrombin Activator Present in Echis Multisquamatus Venom
Thrombosis Research, 1997Co-Authors: Ramona J Petrovan, Götz Nowak, José W. P. Govers-riemslag, Jan Rosing, H. Coenraad Hemker, Guido TansAbstract:Abstract The venom of Echis multisquamatus (Central Asian sand viper) contains a single prothrombin activator, designated multisquamase, which is structurally and functionally different from ecarin, the prothrombin activator from the venom of Echis carinatus (saw-scaled viper). Multisquamase is comprised of a 58000 Mr and a 23000 Mr subunit that consists of two disulfide-linked chains of 12000 Mr and 10000 Mr, respectively. In contrast to ecarin, which activates prothrombin and prethrombin 1 at comparable rates, and whose activity is hardly affected by Ca2+ or by changes in ionic strength, multisquamase hardly activates prethrombin 1; prothrombin activation requires Ca2+ and is strongly inhibited at high ionic strength. The most favourable kinetic parameters are observed at 1 mM Ca2+ and at low ionic strength (Km = 0.085 μM and kcat = 0.68 s−1 at I ≅ 0.04). An increase in ionic strength considerably reduces the rate of prothrombin activation, due to an increase of the Km (Km = 0.8 μM and kcat = 1.03 s−1 at I ≅ 0.2). Studies in plasmas from patients on oral anticoagulant therapy show that E. Multisquamatus venom only activates carboxylated prothrombin, whereas E. carinatus activates both prothrombin and descarboxyprothrombin. Thus, multisquamase-dependent prothrombin activation appears to require post-translational modification of the gla-domain. This venom prothrombin activator may, therefore, become a useful tool to quantitate prothrombin and descarboxyprothrombin in cases where vitamin K-dependent carboxylation of prothrombin is impaired.
Jan Rosing - One of the best experts on this subject based on the ideXlab platform.
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Purification and Characterization of Multisquamase, the Prothrombin Activator Present in Echis Multisquamatus Venom
Thrombosis Research, 1997Co-Authors: Ramona J Petrovan, Götz Nowak, José W. P. Govers-riemslag, Jan Rosing, H. Coenraad Hemker, Guido TansAbstract:Abstract The venom of Echis multisquamatus (Central Asian sand viper) contains a single prothrombin activator, designated multisquamase, which is structurally and functionally different from ecarin, the prothrombin activator from the venom of Echis carinatus (saw-scaled viper). Multisquamase is comprised of a 58000 Mr and a 23000 Mr subunit that consists of two disulfide-linked chains of 12000 Mr and 10000 Mr, respectively. In contrast to ecarin, which activates prothrombin and prethrombin 1 at comparable rates, and whose activity is hardly affected by Ca2+ or by changes in ionic strength, multisquamase hardly activates prethrombin 1; prothrombin activation requires Ca2+ and is strongly inhibited at high ionic strength. The most favourable kinetic parameters are observed at 1 mM Ca2+ and at low ionic strength (Km = 0.085 μM and kcat = 0.68 s−1 at I ≅ 0.04). An increase in ionic strength considerably reduces the rate of prothrombin activation, due to an increase of the Km (Km = 0.8 μM and kcat = 1.03 s−1 at I ≅ 0.2). Studies in plasmas from patients on oral anticoagulant therapy show that E. Multisquamatus venom only activates carboxylated prothrombin, whereas E. carinatus activates both prothrombin and descarboxyprothrombin. Thus, multisquamase-dependent prothrombin activation appears to require post-translational modification of the gla-domain. This venom prothrombin activator may, therefore, become a useful tool to quantitate prothrombin and descarboxyprothrombin in cases where vitamin K-dependent carboxylation of prothrombin is impaired.
