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Published on: July 25, 2014
Determination of the molecular size of the hepatic H1-receptor by target size analysis
Abstract:
The molecular sizes of histamine H1-receptors of rat, rabbit, human, pig, guinea-pig, chicken, dog, and bovine liver were investigated by radiation inactivation and determined to be 100,000 to 160,000 daltons in all the animals examined. Statistical analysis showed that the hepatic H1-receptors have a common size of 128,000 +/- 63,000 daltons. Saturation analysis showed that the [3H]mepyramine binding constant was not changed by irradiation, while the binding capacity decreased with increase in the radiation dose.
Insights
This study determined the molecular size of histamine H1-receptors across multiple animal species. Results indicate a consistent receptor size, with radiation affecting binding capacity but not the binding constant.
Area of Science:
- Pharmacology
- Biochemistry
- Molecular Biology
Background:
- Histamine H1-receptors are crucial in mediating allergic and inflammatory responses.
- Understanding the molecular properties of these receptors is key to developing targeted therapeutics.
Purpose of the Study:
- To determine the molecular size of histamine H1-receptors in various animal livers.
- To investigate the impact of radiation inactivation on receptor binding characteristics.
Main Methods:
- Radiation inactivation assay was employed to determine the molecular size of H1-receptors.
- Saturation analysis was used to assess the effects of irradiation on [3H]mepyramine binding.
Main Results:
- Histamine H1-receptor molecular sizes ranged from 100,000 to 160,000 daltons across species.
- Statistical analysis revealed a common hepatic H1-receptor size of 128,000 +/- 63,000 daltons.
- Irradiation did not alter the [3H]mepyramine binding constant but decreased binding capacity.
Conclusions:
- Hepatic histamine H1-receptors exhibit a conserved molecular size across diverse mammalian and avian species.
- Radiation inactivation is a valid method for assessing receptor size, and its effects on binding parameters provide insights into receptor structure-function relationships.

