Rapid degradation of the silkworm diapause hormone by trypsin and its suppression by VAP-map, a synthetic analog of the cuticular peptide of silkworm, Bm ACP-6.7 (VAP-peptide).
Very fast tryptic degradation of the silkworm diapause hormone was found and the degradation pathway was analyzed by moderating the reaction conditions. It proceeded via cleavage at Arg23 and finally at Arg15 of DH. As the C-terminal structure of DH was essential for exhibiting bioactivity, the first cleavage caused rapid inactivation of the hormone. This tryptic digestion was strongly suppressed by adding VAP-map, a synthetic analog of the cuticular peptide of silkmoths, Bm ACP-6.7 (VAP-peptide), which is a natural synergist of DH. VAP-map suppressed the enzymic reaction by interacting with the substrate, but not with the enzyme.
Baba
H
H
Faculty of Bio-resources, Mie University, Tsu, Japan.
Katsuzaki
H
H
Komiya
T
T
Yamashita
O
O
Imai
K
K
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D006868:Hydrolysis; D007301:Insect Hormones / Q000037:antagonists & inhibitors / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000037:antagonists & inhibitors / Q000378:metabolism*; D010449:Peptide Mapping; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology*; D017386:Sequence Homology, Amino Acid; D014357:Trypsin / Q000378:metabolism*
D007301:Insect Hormones; D009479:Neuropeptides; D010455:Peptides; C438907:VAP-map peptide; C075027:diapause hormone; D014357:Trypsin