Saponinas esteroidais neutras

Froidevaux , R.; Krier , F.; Nedjar-Arroume , N.; Vercaigne-Marko , D.; Kosciarz , E.; Ruckebusch , C.; Dhulster , P.; Guillochon , D.
Peptic digestion of bovine hemoglobin yields a fragment with antibacterial activity. This peptide was purified to homogeneity by a two-step procedure including anion exchange chromatography and preparative reversed-phase HPLC. Mass determination and fragmentation indicated that this peptide corresponded to the 1–23 fragment of the chain of hemoglobin. The minimum inhibitory concentration and mode of action of this peptide towards Micrococcus luteus strain A270 were determined. Hemolytic assay, interaction with liposomes, and study of its structure in solution were also performed.

Saponinas esteroidais neutras

saponinas esteroidais neutras

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saponinas esteroidais neutrassaponinas esteroidais neutrassaponinas esteroidais neutrassaponinas esteroidais neutrassaponinas esteroidais neutras

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