Purification and characterization of a poly-L-lysine-activated serine endoprotease from Lumbricus rubellus.
An endoprotease in earthworm (Lumbricus rubellus) is purified to apparent homogeneity using 125I-lactalbumin as a substrate. The protease has a molecular mass of 27 kDa and is markedly activated by poly-L-lysine or poly-L-arginine. It is a chymotrypsin-like serine protease. Its activity is distributed to coelomic fluid but relatively little to coelomocytes.
Woo
K M
KM
Department of Molecular Biology, College of Natural Sciences, Seoul National University, Korea.
Yi
W
W
Sohn
Y J
YJ
Chang
C S
CS
Kang
M S
MS
Ha
D B
DB
Chung
C H
CH
D000595:Amino Acid Sequence; D000818:Animals; D004789:Enzyme Activation / Q000187:drug effects; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009835:Oligochaeta / Q000201:enzymology*; D010455:Peptides / Q000494:pharmacology; D011107:Polylysine / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D013379:Substrate Specificity
D010455:Peptides; D011107:Polylysine; C015462:polyarginine; D012697:Serine Endopeptidases