Author:
Seely John H.,Benoiton Leo
Abstract
DL-Homolysine was resistant to the action of lysine decarboxylase from Bacterium cadaveris, but was oxidized by L-amino acid oxidase from Crotalus adamanteus. ε-N-Acetyl-DL-homolysine was not hydrolyzed by ε-lysine acylase from hog kidney, but was hydrolyzed by a chicken kidney enzyme preparation. Hog kidney acylase showed slight activity towards α-N,ζ-N-dichloroacetyl- and α-N-chloroacetyl-ζ-N-carbobenzoxy-DL-homolysine. DL-Homolysine ethyl ester was hydrolyzed by trypsin at a rate one-eighth of that for lysine ethyl ester.
Publisher
Canadian Science Publishing
Cited by
4 articles.
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