Inhibition of prophenoloxidase-activating enzyme from Bombyx mori by endogenous chymotrypsin inhibitors.
Inhibitory activities for the activation of prophenoloxidase with its activating enzyme were detected in the gel-filtration fractions of hemolymph from Bombyx mori. The fractions with the highest activity contained chymotrypsin inhibitors; CI-13a, 13b, and 13c. They inhibited the activation of prophenoloxidase. The activating enzyme affected a synthetic substrate for trypsin, Boc-Gln-Ala-Arg-MCA: Km = 0.62 mM. CI-13c partially suppressed the peptidase activity.
Aso
Y
Y
Laboratory of Protein Chemistry and Engineering, Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.
Yamashita
T
T
Meno
K
K
Murakami
M
M
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000201:enzymology*; D004156:Catechol Oxidase / Q000378:metabolism*; D002850:Chromatography, Gel; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D004789:Enzyme Activation / Q000187:drug effects; D004792:Enzyme Precursors / Q000097:blood / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D006458:Hemolymph / Q000201:enzymology; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000097:blood / Q000737:chemistry* / Q000302:isolation & purification; D012697:Serine Endopeptidases; D014361:Trypsin Inhibitors / Q000097:blood / Q000302:isolation & purification / Q000494:pharmacology / Q000502:physiology*
D004792:Enzyme Precursors; D014361:Trypsin Inhibitors; C038451:pro-phenoloxidase; D004156:Catechol Oxidase; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; C022435:prephenoloxidase-activating enzyme; D002918:Chymotrypsin