Abstract
We found an enzyme in the microsomal fraction of 21-day-old-rat liver, which liberates a free aldehyde from 1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine (lysoplasmalogen) and which has an activity of about 42 mU/mg protein under the conditions described. Kinetic data are presented. The pH optimum is found around pH 7.1. SH-blocking reagents, as well as deoxycholate, act as strong inhibitors, while Mg2 and Ca2 also inhibit the reaction to some extent. The enzymic activity is specific with respect to the monoradylphospholipid, since the acylated compound 2-acyl-1-(1-alkenyl)-sn-glycero-3-phosphoethanolamine does not serve as substrate. The ether linkage of 1-alkyl-sn-glycero-3-phosphoethanolamine is not hydrolyzed either under these conditions. A similar enzyme activity in liver has only been described for choline-containing lysoplasmalogen.
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Schedule a callMore From: Hoppe-Seyler's Zeitschrift fur physiologische Chemie
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