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Large-scale purification of hnRNP proteins from HeLa cells by affinity chromatography on ssDNA-cellulose.

par Pandolfo, Massimo ;Valentini, O;Biamonti, G;Rossi, Pier Luca;Riva, S
Référence European journal of biochemistry / FEBS, 162, 1, page (213-220)
Publication Publié, 1987-01

Article révisé par les pairs

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Résumé :

A purification procedure for proteins which bind heterogeneous nuclear RNA (hnRNP proteins) is described. The procedure, which entails standard chromatographic fractionations (single-stranded DNA cellulose, hydroxyapatite) and detection with specific antibodies, allows a large-scale preparation of these proteins and the partial separation of different polypeptides. By this method, polypeptides of higher molecular mass (53-55 kDa) can be purified, which are structurally and antigenically related to the 'canonical' hnRNP core proteins (34-43 kDa) that constitute the 40S hnRNP complexes. We also show that HeLa cells contain a protease that cleaves hnRNP core proteins to discrete smaller polypeptides of 22-28 kDa. Such protease, which has been partially purified, appears to copurify extensively with some of the hnRNP proteins.