Modulation of lysyl oxidase substrate specificity by the oleate anion.
Extracts of bovine ligamentum nuchae have been assayed for lysyl oxidase activity using as substrates soluble elastin and soluble collagen labeled with tritiated lysine. The assays were performed in the presence and absence of sodium oleate. At 0.8 mM, oleate decreased activity with elastin more than 50% and enhanced activity with collagen to approximately 200% that of controls without oleate. The results show that this hydrophobic anion modulates lysyl oxidase specificity in crude extracts and suggests a mechanism for modifying activity in tissues.
Losty
T A
TA
Miller
D S
DS
O'Dell
B L
BL
D000594:Amino Acid Oxidoreductases / Q000032:analysis*; D000818:Animals; D002417:Cattle; D003094:Collagen; D004549:Elastin; D019301:Oleic Acid; D009829:Oleic Acids / Q000494:pharmacology*; D008249:Protein-Lysine 6-Oxidase / Q000032:analysis*; D013379:Substrate Specificity
D009829:Oleic Acids; D019301:Oleic Acid; D003094:Collagen; D004549:Elastin; D000594:Amino Acid Oxidoreductases; D008249:Protein-Lysine 6-Oxidase