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| Item Type: | Article |
|---|---|
| Title: | Resolution of transducin subunits by chromatography on blue sepharose |
| Creators Name: | Kleuss, C., Pallast, M., Brendel, S., Rosenthal, W. and Schultz, G. |
| Abstract: | The retinal guanine nucleotide-binding protein, transducin (TD), was subjected to chromatography on Blue Sepharose (BLS). A simple two-step protocol was developed, allowing the resolution of the alpha-subunit and the beta gamma-complex of the protein extracted from bovine retina by the use of a poorly hydrolysable GTP analogue. If TD was applied to BLS in a divalent cation-containing buffer, the beta gamma-complex did not bind to the resin, whereas the alpha-subunit was retained; elution of the latter was achieved by removing the divalent cation from the buffer. Binding of the alpha-subunit to BLS was not affected by nucleotides or by ADP ribosylation catalysed by bacterial toxins. However, adsorption of the alpha-subunit by BLS or by a strong cation exchanger (Mono S) depended strictly on divalent cations. In contrast to previous reports, the data suggest the formation of a complex between a sulphonyl residue of Cibacron Blue, a divalent metal ion, and the alpha-subunit as the relevant binding mechanism causing adsorption of the alpha-subunit to BLS. |
| Keywords: | Ion Exchange Chromatography, Guanosine 5'-O-(3-Thiotriphosphate), Guanosine Triphosphate, Membrane Proteins, Retina, Sepharose, Sulfur Radioisotopes, Thionucleotides, Transducin, Animals, Cattle |
| Source: | Journal of chromatography |
| ISSN: | 0021-9673 |
| Publisher: | Elsevier |
| Volume: | 407 |
| Page Range: | 281-289 |
| Date: | 16 October 1987 |
| Official Publication: | https://doi.org/10.1016/S0021-9673(01)92625-1 |
| PubMed: | View item in PubMed |
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