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Comparative Study
. 1984 Oct 23;790(2):174-81.
doi: 10.1016/0167-4838(84)90221-8.

Purification and characterization of a basic 23 kDa cytosolic protein from bovine brain

I Bernier, P Jollès
Comparative Study

Purification and characterization of a basic 23 kDa cytosolic protein from bovine brain

I Bernier et al. Biochim Biophys Acta. .

Abstract

A soluble basic protein has been purified from bovine brain. It is constituted by a single polypeptide chain with a molecular weight of about 23 kDa and an isoelectric point of about 8.6. The protein was further characterized by its amino-acid composition and by a 39 amino-acid-long N-terminal sequence. Sequence homologies were demonstrated with some other cytosolic proteins. Ligand-binding assays revealed a significant affinity of the 23 kDa protein for bromosulfophthalein. Immunochemical analysis using a rabbit anti 23 kDa brain protein antiserum demonstrated its simultaneous presence in bovine liver as well as in soluble extracts from different origins (mouse and rat brain; human platelets).

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