vinca difformis/albumin

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Binding of vinca alkaloid analogues to human serum albumin and to alpha 1-acid glycoprotein.

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The binding of a series of vinca alkaloid analogues having eburnane or indolo[2,3-a]quinolizidine skeletons was studied with human serum albumin (HSA) by affinity chromatography and with alpha 1-acid glycoprotein by means of competition experiments. On HSA the binding occurs at the

Chiral high-performance liquid chromatographic separations of vinca alkaloid analogues on alpha 1-acid glycoprotein and human serum albumin columns.

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Separations of the stereoisomers of a series of tetracyclic and pentacyclic vinca alkaloid analogues having two or three chiral centres were performed on Chiral-AGP and Chiral-HSA high-performance liquid chromatographic columns. Phosphate buffers with pH 5-7 containing 5-35% acetonitrile or

Monoclonal antibodies to antitumor Vinca alkaloids: thermodynamics and kinetics.

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Spleen cells from a mouse and a rat immunized with vinblastine coupled to bovine serum albumin were fused in two independent experiments with P3 X 63-Ag8 (non-secreting variant) mouse myeloma cells. Three mouse X mouse (Vinca 1-3) and two rat X mouse (Vinca 4 and 5) hybrids were selected for

Vinca-23-oyl amino acid derivatives: as new anticancer agents (review).

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Vinblastine-23-oyl amino acid derivatives and the analog deoxy vinblastine derivative were synthesized by linking amino acid carbocyclic esters to the vinca-23-oyl moiety, through an amide linkage. Their experimental chemotherapeutic activities on P388, L1210 leukemias and 6C3HED lymphosarcoma in

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