- 【Updated on May 12, 2025】 Integration of CiNii Dissertations and CiNii Books into CiNii Research
- Trial version of CiNii Research Automatic Translation feature is available on CiNii Labs
- Suspension and deletion of data provided by Nikkei BP
- Regarding the recording of “Research Data” and “Evidence Data”
Solubilization, characterization and partial purification of (3H)mepyramine-binding protein, a possible histamine H1 receptor, from rat liver membrane.
-
- FUKUI Hiroyuki
- Department of Pharmacology II, Osaka University School of Medicine
-
- WANG Nai Ping
- Department of Pharmacology II, Osaka University School of Medicine
-
- WATANABE Takehiko
- Department of Pharmacology I, Tohoku University School of Medicine
-
- WADA Hiroshi
- Department of Pharmacology II, Osaka University School of Medicine
Search this article
Description
[3H] Mepyramine binding protein, a possible subtype of histamine H, receptors, was solubilized from rat liver membrane with 3-[(3-cholamidopropyl)-dimethylammonio] -1 -propanesulfonate (CHAPS) and Tween 60 as detergents and glycerol as an enhancer of solubilization. The optimal concentration of CHAPS was 10 mM and that of glycerol was 20% or more (v/v). The molecular weight of the [3H]mepyramine binding protein-detergent complex was determined to be 670K by Sepharose CL-4B gel filtration and 800K by sucrose density gradient sedimentation. By target size analysis, the molecular weights of both the membranebound and solubilized [3H]mepyramine binding protein were determined to be 162K. These values are similar to those of other well-characterized H, -receptor proteins, though slightly different. Simultaneous computerized analysis of the data obtained by [3H]mepyramine binding to the solubilized [3H]mepyramine binding protein indicated the presence of a single binding site with a KD value of 19.0±5.6 nM and a binding capacity (Bmax) of 6.6±2.1 pmole/mg protein. The Ki value of cold mepyramine for [3H]mepyramine binding to the solubilized receptor was 20±4 nM, whereas those of diphenhydramine, d-chlorpheniramine and triprolidine were all 2.9±0.8 μM, or about 150 times that of mepyramine. These data on the molecular and binding characteristics of the solubilized protein reported here suggest that there is a subtype of histamine H1 receptor in rat liver membrane. The solubilized preparation retained 90% and 75% of its [3H]mepyramine binding activity after storage at -80°C and 4°C, respectively, for 20 days. The solubilized [3H]mepyramine binding protein was purified 30-fold by Sepharose CL-4B gel filtration, Bio Gel HTP hydroxylapatite, Octyl Sepharose 4B and hydroxylapatite HPLC column chromatographies.
Journal
-
- The Japanese Journal of Pharmacology
-
The Japanese Journal of Pharmacology 46 (2), 127-139, 1988
The Japanese Pharmacological Society
- Tweet
Keywords
Details 詳細情報について
-
- CRID
- 1390001204289103616
-
- NII Article ID
- 130000832101
-
- COI
- 1:CAS:528:DyaL1cXhtVKqtL8%3D
-
- ISSN
- 13473506
- 00215198
-
- PubMed
- 3379823
-
- Text Lang
- en
-
- Article Type
- journal article
-
- Data Source
-
- JaLC
- Crossref
- PubMed
- CiNii Articles
- OpenAIRE
-
- Abstract License Flag
- Disallowed