Isolation and partial structure of a unique lipophilic peptide, VAP peptide, from the heads of male silkworm moths.
A new lipophilic peptide was isolated from the MeOH-CH2Cl2 extract of adult heads of the male silkworm, Bombyx mori, by monitoring the diapause egg-inducing activity. Partial amino acid sequencing (1-55) revealed this peptide to be a unique type having a high content of lipophilic amino acids, Val, Ala, and Pro, and many repeating sequences. The compound was thus named VAP peptide.
Imai
K
K
School of Bioresources, Mie University, Japan.
Sugiura
K
K
Komiya
T
T
Yamashita
O
O
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx / Q000737:chemistry*; D007301:Insect Hormones / Q000032:analysis / Q000302:isolation & purification / Q000502:physiology; D008297:Male; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000032:analysis / Q000302:isolation & purification* / Q000502:physiology
D007301:Insect Hormones; D009479:Neuropeptides; C115047:VAP peptide