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BIOCHEMICAL AND IMMUNOLOGICAL CHARACTERIZATION OF ALKALOID‐BINDING PROTEINS FROM IMMATURE RAT BRAIN 1
Author(s) -
Twomey S. L.,
Raeburn S.,
Baxter C. F.
Publication year - 1976
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1976.tb01558.x
Subject(s) - vinblastine , colchicine , sephadex , binding protein , tubulin , biochemistry , antiserum , antibody , biology , isoelectric focusing , chemistry , protein a/g , microbiology and biotechnology , microtubule , immunology , enzyme , recombinant dna , genetics , chemotherapy , gene , fusion protein
— Vinblastine‐ and colchicine‐binding proteins in the soluble fraction of immature rat brains were characterized and compared. Based upon criteria of Sephadex G‐200 chromatography, electrofocusing and immunological reactivity, several separable species of vinblastine‐binding protein were isolated. By contrast, these same procedures yielded only one protein band or elution peak to which [ 14 C]colchicine could be tightly bound. This colchicine‐binding protein peak coincided, in part, with one of the protein peaks to which [ 3 H]vinblastine was tightly bound. Rabbit antiserum against soluble brain proteins precipitated by vinblastine sulfate contained antibodies which reacted with colchicine‐binding protein. Thus, despite apparent differences in physical properties between the bulk of the vinblastine‐binding proteins and the colchicine‐binding protein, the vinblastine sulfate‐precipitated protein antigens gave rise to antibodies capable of forming an immune complex with colchicine‐binding protein.