Isolation of sodium-complexing polypeptides from mammalian blood and cardiac muscle

Summary Two distinct polypeptides have been isolated from rat heart and ox blood. They are both found to be effective in forming complexes with sodium ions, and it is suggested that they may have a function in stabilizing sodium ion activity.Acknowledgments. We are indebted to ProfessorG. A. Gilbert, F.R.S. and to Dr.C. J. Lote for helpful discussion, and to the Royal Society for a Grant-in-aid which in part supported the investigation.     

The acetylatin of tryptophan metabolites by rapid and slow acetylators of sulfamethazine

Zusammenfassung Es wurden an gesunden Versuchspersonen Belastungsversuche mit Sulfamethazin und Tryptophan ausgeführt und die Ausscheidung der azetylierten Metaboliten im Harn verfolgt. Bei den Tryptophanmetaboliten Kynurenin und Hydroxykynurenin war — im Gegensatz zur Azetylierung von Sulfamethazin — kein Polymorphismus zu beobachten.     

Conformations and biological properties of apomorphine and its phenanthro(10,1-b,c)azepine homologue.

11,12-Dihydroxy-7-methyl-4,5,6,7,7a,8-hexahydrophenanthro[10,1-b,c]-azepine (2), a homologue of apomorphine (1), has been found to be devoid of dopaminergic effects. The biological differences between apomorphine and this homologue are explained in terms of differences in conformation of the two molecules.