PROIMI   05436
PLANTA PILOTO DE PROCESOS INDUSTRIALES MICROBIOLOGICOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
10. “Activation of Limulus Coagulation Factor G by Scleroglucan as a Biological Activity Measurement”
Autor/es:
S.C. VIÑARTA; I.M. VIRGILI ALEMAN; L.I.C. FIGUEROA; J.I. FARIÑA
Lugar:
Chubut
Reunión:
Congreso; . XLVI Reunión Anual Sociedad Argentina de Investigación Bioquímica (SAIB 2010); 2010
Resumen:
The ability of scleroglucan (b-1,3-b-1,6 glucan) conformers to activate Limulus coagulation factor G was evaluated. Studies pursued to get a further insight into the scleroglucan structure-function relationship. Labscale produced (EPS I, EPS II, EPSi) and commercial (LSCL) scleroglucans were tested on their ability to activate factor G of the Limulus coagulation cascade (Glucatell Test, Pyrolab). Native triplex conformation was obtained by dissolving scleroglucan (2 pg/mL) in distilled water. Thermally- (150°C, 30 min) and al kali-treated (0·2 N NaOH, 10 min) scleroglucans were also prepared. Single helices were further evaluated at 2 ng/mL and 2 ìg/mL. All scleroglucans were endotoxin-free (LAL-Test, Pyrolab). Triplex conformation had stronger ability to activate factor G than single helix, with EPS I and EPS II as the most active polymers. Thermal and alkaline denaturation significantly reduced scleroglucan reactivity, being EPS II the most stable glucan, whilst EPSi and LSCL were the most affected ones (91-99% reduction). Single helix activation ability was significantly dependent on polysaccharide concentration. Scleroglucans from S. rolfsii ATCC 201126 (EPS I and EPS II) exhibited marked clotting activity against factor G and were more effective than commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. was obtained by dissolving scleroglucan (2 pg/mL) in distilled water. Thermally- (150°C, 30 min) and al kali-treated (0·2 N NaOH, 10 min) scleroglucans were also prepared. Single helices were further evaluated at 2 ng/mL and 2 ìg/mL. All scleroglucans were endotoxin-free (LAL-Test, Pyrolab). Triplex conformation had stronger ability to activate factor G than single helix, with EPS I and EPS II as the most active polymers. Thermal and alkaline denaturation significantly reduced scleroglucan reactivity, being EPS II the most stable glucan, whilst EPSi and LSCL were the most affected ones (91-99% reduction). Single helix activation ability was significantly dependent on polysaccharide concentration. Scleroglucans from S. rolfsii ATCC 201126 (EPS I and EPS II) exhibited marked clotting activity against factor G and were more effective than commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. produced (EPS I, EPS II, EPSi) and commercial (LSCL) scleroglucans were tested on their ability to activate factor G of the Limulus coagulation cascade (Glucatell Test, Pyrolab). Native triplex conformation was obtained by dissolving scleroglucan (2 pg/mL) in distilled water. Thermally- (150°C, 30 min) and al kali-treated (0·2 N NaOH, 10 min) scleroglucans were also prepared. Single helices were further evaluated at 2 ng/mL and 2 ìg/mL. All scleroglucans were endotoxin-free (LAL-Test, Pyrolab). Triplex conformation had stronger ability to activate factor G than single helix, with EPS I and EPS II as the most active polymers. Thermal and alkaline denaturation significantly reduced scleroglucan reactivity, being EPS II the most stable glucan, whilst EPSi and LSCL were the most affected ones (91-99% reduction). Single helix activation ability was significantly dependent on polysaccharide concentration. Scleroglucans from S. rolfsii ATCC 201126 (EPS I and EPS II) exhibited marked clotting activity against factor G and were more effective than commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. was obtained by dissolving scleroglucan (2 pg/mL) in distilled water. Thermally- (150°C, 30 min) and al kali-treated (0·2 N NaOH, 10 min) scleroglucans were also prepared. Single helices were further evaluated at 2 ng/mL and 2 ìg/mL. All scleroglucans were endotoxin-free (LAL-Test, Pyrolab). Triplex conformation had stronger ability to activate factor G than single helix, with EPS I and EPS II as the most active polymers. Thermal and alkaline denaturation significantly reduced scleroglucan reactivity, being EPS II the most stable glucan, whilst EPSi and LSCL were the most affected ones (91-99% reduction). Single helix activation ability was significantly dependent on polysaccharide concentration. Scleroglucans from S. rolfsii ATCC 201126 (EPS I and EPS II) exhibited marked clotting activity against factor G and were more effective than commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. b-1,3-b-1,6 glucan) conformers to activate Limulus coagulation factor G was evaluated. Studies pursued to get a further insight into the scleroglucan structure-function relationship. Labscale produced (EPS I, EPS II, EPSi) and commercial (LSCL) scleroglucans were tested on their ability to activate factor G of the Limulus coagulation cascade (Glucatell Test, Pyrolab). Native triplex conformation was obtained by dissolving scleroglucan (2 pg/mL) in distilled water. Thermally- (150°C, 30 min) and al kali-treated (0·2 N NaOH, 10 min) scleroglucans were also prepared. Single helices were further evaluated at 2 ng/mL and 2 ìg/mL. All scleroglucans were endotoxin-free (LAL-Test, Pyrolab). Triplex conformation had stronger ability to activate factor G than single helix, with EPS I and EPS II as the most active polymers. Thermal and alkaline denaturation significantly reduced scleroglucan reactivity, being EPS II the most stable glucan, whilst EPSi and LSCL were the most affected ones (91-99% reduction). Single helix activation ability was significantly dependent on polysaccharide concentration. Scleroglucans from S. rolfsii ATCC 201126 (EPS I and EPS II) exhibited marked clotting activity against factor G and were more effective than commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. was obtained by dissolving scleroglucan (2 pg/mL) in distilled water. Thermally- (150°C, 30 min) and al kali-treated (0·2 N NaOH, 10 min) scleroglucans were also prepared. Single helices were further evaluated at 2 ng/mL and 2 ìg/mL. All scleroglucans were endotoxin-free (LAL-Test, Pyrolab). Triplex conformation had stronger ability to activate factor G than single helix, with EPS I and EPS II as the most active polymers. Thermal and alkaline denaturation significantly reduced scleroglucan reactivity, being EPS II the most stable glucan, whilst EPSi and LSCL were the most affected ones (91-99% reduction). Single helix activation ability was significantly dependent on polysaccharide concentration. Scleroglucans from S. rolfsii ATCC 201126 (EPS I and EPS II) exhibited marked clotting activity against factor G and were more effective than commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. Limulus coagulation cascade (Glucatell Test, Pyrolab). Native triplex conformation was obtained by dissolving scleroglucan (2 pg/mL) in distilled water. Thermally- (150°C, 30 min) and al kali-treated (0·2 N NaOH, 10 min) scleroglucans were also prepared. Single helices were further evaluated at 2 ng/mL and 2 ìg/mL. All scleroglucans were endotoxin-free (LAL-Test, Pyrolab). Triplex conformation had stronger ability to activate factor G than single helix, with EPS I and EPS II as the most active polymers. Thermal and alkaline denaturation significantly reduced scleroglucan reactivity, being EPS II the most stable glucan, whilst EPSi and LSCL were the most affected ones (91-99% reduction). Single helix activation ability was significantly dependent on polysaccharide concentration. Scleroglucans from S. rolfsii ATCC 201126 (EPS I and EPS II) exhibited marked clotting activity against factor G and were more effective than commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration. S. rolfsii ATCC 201126 (EPS I and EPS II) exhibited marked clotting activity against factor G and were more effective than commercial scleroglucan. Denaturation would lead to lower biological activity and it would be dependent on EPS concentration.