Purification and characterization of two serine protease inhibitors from the hemolymph of Mythimna unipuncta.
Two serine protease inhibitors, trypsin inhibitor and alpha-chymotrypsin inhibitor, were isolated from the hemolymph of Mythimna unipuncta. Mythimna trypsin and alpha-chymotrypsin inhibitors were purified by gel filtration and anion-exchange chromatography. They displayed molecular masses of 52 kDa and 43 kDa, respectively, as determined by electrophoresis under reducing and non-reducing conditions on denaturing polyacrylamide gels. Their isoelectric points were evaluated by isoelectric focusing and two-dimensional electrophoresis. Their N-terminal sequences have been analyzed as APSDTTIAETLTITEEFFPD and FDESFGFQGPSTYEKTPLGEP, respectively. The role of these inhibitors in the regulation of the defense reaction of the insect is discussed.
Cherqui
A
A
Departamento da Biologia, Universidade dos Açores, Rua Mãe Deus, 9500 Ponta Delgada, Portugal. anas.cherqui@u-picardie.fr
Cruz
N
N
Simões
N
N
D000595:Amino Acid Sequence; D000818:Animals; D002918:Chymotrypsin / Q000037:antagonists & inhibitors; D006458:Hemolymph / Q000737:chemistry; D019476:Insect Proteins / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D009036:Moths / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000097:blood; D014361:Trypsin Inhibitors / Q000097:blood*
D019476:Insect Proteins; D015842:Serine Proteinase Inhibitors; D014361:Trypsin Inhibitors; D002918:Chymotrypsin