Degradation of side-chains of N-(2-hydroxypropyl)methacrylamide copolymers by lysosomal thiol-proteinases.
N-(2-Hydroxypropyl)methacrylamide copolymers bearing oligopeptide side-chains terminating in p-nitroaniline (NAp) were incubated with rat liver lysosomal enzymes in the presence of the thiol glutathione, and the rate of p-nitroaniline release was measured. Twelve of the 16 side-chains investigated were hydrolysed to release p-nitroaniline and in all but one case degradation was partially or totally inhibited by leupeptin. The effect of substrate concentration on the degradation of the most readily cleaved side-chain, -Ala-Gly-Val-Phe-NAp, was measured.
D000178:Acrylamides / Q000378:metabolism*; D000818:Animals; D003546:Cysteine Endopeptidases; D010450:Endopeptidases / Q000378:metabolism*; D066298:In Vitro Techniques; D007976:Leupeptins / Q000494:pharmacology; D008099:Liver / Q000201:enzymology / Q000378:metabolism; D008247:Lysosomes / Q000201:enzymology*; D011108:Polymers / Q000378:metabolism; D051381:Rats
D000178:Acrylamides; D007976:Leupeptins; D011108:Polymers; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; C032976:N-(2-hydroxypropyl)methacrylamide