Aminopeptidase P from bovine lung: solubilization, properties, and potential role in bradykinin degradation.

Aminopeptidase P was solubilized from bovine lung by sodium deoxycholate extraction of salt-washed, delipidated lung acetone powders. Hydrolysis of the standard aminopeptidase P substrate, Gly-Pro-Hyp, as well as cleavage of Arg-Pro-Pro and the Arg1-Pro2 bond of bradykinin, co-eluted from a Mono Q anion exchange column and demonstrated identical inhibitory profiles suggesting that all activities were functions of the same enzyme. The metal chelator, 1,10-phenanthroline, completely inhibited activity suggesting that aminopeptidase P is a metallopeptidase.

Investigations on myelination in vitro: IV. "Myelin-like" or premyelin structures in cultures of dissociated brain cells from 14--15-day-old embryonic mice.

The present study reports ultrastructural and biochemical data characteristic of myelin-related structures in 30- to 41-day-old cultures of dissociated brain cells from 14- to 15-day-old embryonic mice. Multilayered membranous material was identified and displayed an alternation of electron-lucent and electron-dense lamellae with a periodicity of 102 A. In these membranes, typical myelin constituents like basic protein, cerebrosides, sulfatides, and CNPase could be identified.

Concanavalin A-binding glycopeptides from rat brain glycoproteins.

The affinity of concanavalin A for neutral and acidic glycopeptides derived from rat brain glycoproteins was investigated by studying the inhibition of a concanavalin A-glycogen precipitation system. The neutral, mannose-rich glycopeptides obtained by column electrophoresis of the dialyzable glycopeptides that had been solubilized by proteolytic treatment of defatted brain tissue were powerful inhibitors, with an inhibitory activity 20 to 26 times that of the standard inhibitor, methyl-alpha-D-mannoside. The acidic sialoglycopeptides had activities one to nine times that of the mannoside.