English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

In a foregoing paper (1), a method for labeling histamine Ht receptor with radioactive dibenamine in the smooth muscle of cat small intestine was proposed. We found 7 p moles bound dibenamine per mg protein of the total tissue homogenate and 40 p moles per mg protein of the plasma membrane fraction. This communication deals with reconsideration on the receptor specificity of this bound dibenamine or, more accurately, on the selectivity of Hi receptor. The procedure in the previous paper (1) involved ‘double protection’ which means the two-step application of protectors against dibenamine: the first protection was the usual one with protective antihistamine, promethazine, and the second was cross protection of non-specific sites with drugs having negligible antihistaminic actions in the doses used, thioridazine and atropine. Muscle strips protected with promethazine against non-radioactive dibenamine were treated with 3H-dibenamine in the presence of these second protectors. The second protectors were to cover non-specific sites which had been protected non-speciflcally with promethazine from non-radioactive dibenamine. The first non-radioactive dibenamine was 4 times higher in concentration than the second 3H-dibenamine.

Purification of histamine receptor. VII. Reassessment of specificity of radioactive dibenamine to label H1 receptors.