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Renal V2 vasopressin receptor proteins: identification and enrichment

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Fahrenholz,  Falk
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Kojro,  Elzbieta
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Plage,  G.
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Müller,  M.
Emeritusgroup Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Fahrenholz, F., Kojro, E., Plage, G., & Müller, M. (1988). Renal V2 vasopressin receptor proteins: identification and enrichment. Journal of receptor research, 8(1-4), 283-294. doi:10.3109/10799898809048993.


Cite as: https://hdl.handle.net/21.11116/0000-0009-1591-B
Abstract
The synthesis of the tritium labelled photoreactive analogue of 1-deamino-vasopressin [1-(3-mercaptopropionic acid, 8-(N6-4-azido-phenylamidino)-lysine] vasopressin is described. This analogue retains a high affinity for hepatic V1 and renal V2 vasopressin receptors (apparent dissociation constant KD approximately 1-2 nM). A membrane protein from bovine kidney and pig kidney with an apparent relative molecular mass (Mr) of 30,000 was preferentially labelled and with lower yield a protein band with a Mr-value of 50,000 to 60,000. The photolabelled 30,000-Mr protein from bovine kidney was enriched by size-exclusion chromatography and by reversed-phase-high-performance liquid chromatography.