PROIMI   05436
PLANTA PILOTO DE PROCESOS INDUSTRIALES MICROBIOLOGICOS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Activation of limulus coagulation factor g by scleroglucan as a biological activity measurement
Autor/es:
VIÑARTA S.C,; VIRGILI ALEMÁN IM; CASTELLANOS DE FIGUEROA, LUCÍA INÉS; FARIÑA J.I,
Lugar:
Puerto Madryn, Chubut, Argentina
Reunión:
Congreso; 46th Reunión Anual Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2010
Institución organizadora:
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular
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.
Lab-scale 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
alkali-treated (0·2 N NaOH, 10 min) scleroglucans were also prepared. Single
helices were further evaluated at 2 ng/mL and 2 µg/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.