Role of silicon on oxide morphology and pickling behaviour of automotive steels
- 作者：A. Chattopadhyay ; T. Ch ; a
- 关键词：Fayalite ; Oxide ; Pickling ; Automotive steel
- 刊名：Scripta Materialia
- 出版年：2008
- 期刊代码：157_13596462
- 类别：et
- 出版时间：May 2008
- 卷：58
- 期：10
- 页码：882-885
- 文件大小：549 K
摘要
The pharmacological profiles of 
1-adrenoceptors for ketanserin, prazosin, silodosin, and BMY 7378 (8-[2-[4-(2-methoxyphenyl)-1-piperazinyl]ethyl]-8-azaspiro[4,5]decane-7,9-dione dihydrochloride) were examined under different assay conditions. Among the tested antagonists and 1-adrenoceptors subtypes, ketanserin showed significantly lower affinity for the 1B-adrenoceptor subtype in intact tissue sampled from the rat tail artery, thoracic aorta, and cerebral cortex (functional pKB and binding pKi were approximately 6), than in cerebral cortex membrane preparations or whole cell and membrane preparations of 1B-adrenoceptor transfected Human Embryonic Kidney 293T (HEK 293T) cells (pKi was approximately 8). In these tissues and cells, however, ketanserin showed a similar affinity (pKi = approximately 8) for 1A- and 1D-adrenoceptors even though the assays were conducted under different conditions. In contrast, the affinities of 1A-, 1B-, and 1D-adrenoceptors for prazosin, silodosin, and BMY 7378 did not significantly change under different assay conditions and in different tissues. The present study reveals that the pharmacological profiles of native 1B-adrenoceptors for ketanserin is strongly influenced by the assay conditions and suggest that antagonist affinity is not necessarily constant.
1-adrenoceptors for ketanserin, prazosin, silodosin, and BMY 7378 (8-[2-[4-(2-methoxyphenyl)-1-piperazinyl]ethyl]-8-azaspiro[4,5]decane-7,9-dione dihydrochloride) were examined under different assay conditions. Among the tested antagonists and 1-adrenoceptors subtypes, ketanserin showed significantly lower affinity for the 1B-adrenoceptor subtype in intact tissue sampled from the rat tail artery, thoracic aorta, and cerebral cortex (functional pKB and binding pKi were approximately 6), than in cerebral cortex membrane preparations or whole cell and membrane preparations of 1B-adrenoceptor transfected Human Embryonic Kidney 293T (HEK 293T) cells (pKi was approximately 8). In these tissues and cells, however, ketanserin showed a similar affinity (pKi = approximately 8) for 1A- and 1D-adrenoceptors even though the assays were conducted under different conditions. In contrast, the affinities of 1A-, 1B-, and 1D-adrenoceptors for prazosin, silodosin, and BMY 7378 did not significantly change under different assay conditions and in different tissues. The present study reveals that the pharmacological profiles of native 1B-adrenoceptors for ketanserin is strongly influenced by the assay conditions and suggest that antagonist affinity is not necessarily constant.