TY - JOUR
T1 - Further Characterization of Earthworm Serine Proteases
T2 - Cleavage Specificity Against Peptide Substrates and on Autolysis
AU - Nakajima, Nobuyoshi
AU - Sugimoto, Manabu
AU - Ishihara, Kohji
AU - Nakamura, Kaoru
AU - Hamada, Hiroki
PY - 1999/1/1
Y1 - 1999/1/1
N2 - Cleavage specificity of two fibrinolytic enzymes from Lumbricus rubellus [Nakajima, N., et al., Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993) and 60, 293-300 (1996)] was investigated using β-amyloid 1-40 and oxidized insulin B-chain as peptide substrates. The serine protease, F-III-2, cleaved the former substrate at six sites, and the latter at five sites. F-II digested them at six and ten, respectively. The cleavage specificity of F-III-2 resembled those of both trypsin and chymotrypsin. F-II had a broader specificity than F-III-2 and preferred also the bonds consisting neutral or hydrophobic amino acids. Furthermore, F-III-2 itself was digested initially on the site of Arg(144)-Tyr(145) to produce two peptide fragments, when it was autolyzed regularly by heating.
AB - Cleavage specificity of two fibrinolytic enzymes from Lumbricus rubellus [Nakajima, N., et al., Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993) and 60, 293-300 (1996)] was investigated using β-amyloid 1-40 and oxidized insulin B-chain as peptide substrates. The serine protease, F-III-2, cleaved the former substrate at six sites, and the latter at five sites. F-II digested them at six and ten, respectively. The cleavage specificity of F-III-2 resembled those of both trypsin and chymotrypsin. F-II had a broader specificity than F-III-2 and preferred also the bonds consisting neutral or hydrophobic amino acids. Furthermore, F-III-2 itself was digested initially on the site of Arg(144)-Tyr(145) to produce two peptide fragments, when it was autolyzed regularly by heating.
KW - Cleavage specificity
KW - Earthworm
KW - Fibrinolytic enzyme
KW - Serine protease
KW - β-amyloid
UR - http://www.scopus.com/inward/record.url?scp=0033217531&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033217531&partnerID=8YFLogxK
U2 - 10.1271/bbb.63.2031
DO - 10.1271/bbb.63.2031
M3 - Article
C2 - 10635572
AN - SCOPUS:0033217531
SN - 0916-8451
VL - 63
SP - 2031
EP - 2033
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 11
ER -