Tryptic and chymotryptic proteases released by larvae of the blowfly, Lucilia cuprina.
Proteases released by larvae of the sheep blowfly have been suggested to have a primary role in wound formation and larval nutrition. Assays were carried out on two larval products to analyse the substrate specificity of these proteases, their abundance and approximate molecular weights. Tryptic and chymotryptic activities were found in both products though there were more chymotrypsin-like enzymes in products from 48 h cultures (CESP) than in product collected direct from 48 h larvae (LESP). Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) gels incubated with azocasein showed plaques of major enzyme activity at molecular weights of 20,000 and 26,000 in LESP and at 20,000 in CESP, SDS-PAGE gels, when reacted with peptide substrates showed tryptic activity at 20,000 and 26,000 in LESP, whereas CESP showed only chymotryptic activity at 20,000 and higher molecular weights. The results suggest at least three enzymes, a trypsin and chymotrypsin in LESP, a chymotrypsin in CESP and a tryptic enzyme which is not stable to SDS-PAGE probably in both LESP and CESP. In addition, reactivity with elastase and plasmin substrates suggests the presence of enzymes with general effects on skin substrates and inflammatory pathways.
Sandeman
R M
RM
School of Agriculture, La Trobe University, Bundoora, Victoria, Australia.
Feehan
J P
JP
Chandler
R A
RA
Bowles
V M
VM
D000818:Animals; D002918:Chymotrypsin / Q000737:chemistry*; D004175:Diptera / Q000201:enzymology*; D007814:Larva / Q000201:enzymology; D008970:Molecular Weight; D013379:Substrate Specificity; D014357:Trypsin / Q000737:chemistry*
D002918:Chymotrypsin; D014357:Trypsin