Isolation of a sulfobromophthalein binding protein from hepatocyte plasma membrane
| Autor: | Claudio Tiribelli, Gianfranco Liut, Gabriella Sandri, Giancarlo Lunazzi, Gian Luigi Sottocasa, Bruno Gazzin, Enrico Panfili, Maria Luciani |
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| Přispěvatelé: | Tiribelli, Claudio, Lunazzi, G. C., Luciani, M., Panfili, E., Gazzin, B., Liut, G. F., Sandri, G., Sottocasa, G. L. |
| Jazyk: | angličtina |
| Rok vydání: | 1978 |
| Předmět: |
Chromatography
Binding protein Cell Membrane Membrane Proteins Biochemistry Genetics and Molecular Biology (miscellaneous) Rats Sulfobromophthalein Molecular Weight Dissociation constant Kinetics chemistry.chemical_compound Membrane medicine.anatomical_structure Liver Biochemistry chemistry Hepatocyte Protein purification medicine Acetone Animals Carrier Proteins Polyacrylamide gel electrophoresis |
| Popis: | This paper deals with the isolation and partial characterization of a protein capable of high affinity sulfobromophthalein-binding from liver plasma membrane. The purification involves acetone powder of a crude preparation of rat liver plasma membrane, salt extraction and purification through two chromatographic steps. Based on sulfobromophthalein binding, the process gives a yield of approximately 40%, with a purification of about 300 times with respect to the starting homogenate. The best preparation can bind more than 100 nmol sulfobromophthalein/mg protein. The protein behaves as a single species in dodecyl sulphate polyacrylamide gel electrophoresis, with an apparent molecular weight of 1.7 · 105. The molecule does not contain sugars. The dissociation constant of the protein · sulfobromophthalein complex has been found to be 4 · 10−6 M, a value in agreement with that of high affinity binding sites described on isolated liver plasma membrane. |
| Databáze: | OpenAIRE |
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