Purification and partial amino acid sequence of initiatorin, a prostatic endopeptidase of the silkworm, Bombyx mori.
We have purified initiatorin, a prostatic endopeptidase that initiates the protein-arginine degradation cascade in the spermatophore of Bombyx mori. Purification of the enzyme from spermatophores was monitored by measuring BAEE (N alpha-benzoyl-L-arginine-ethyl ester) hydrolyzing activity. Spermatophores were used as a source for this enzyme. Of several isoforms the major form (MW, 29 kDa) was purified over 200-fold. The N-terminal sequence of initiatorin showed strong homology with those of serine-type of endopeptidases.
Aigaki
T
T
Department of Biology, Tokyo Metropolitan University, Japan.
Kasuga
H
H
Nagaoka
S
S
Osanai
M
M
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001120:Arginine / Q000031:analogs & derivatives / Q000378:metabolism; D012831:Bombyx / Q000201:enzymology*; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011467:Prostate / Q000201:enzymology; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013093:Spermatogonia / Q000201:enzymology*; D013379:Substrate Specificity
D000596:Amino Acids; D001120:Arginine; C009727:benzoylarginine ethyl ester; D012697:Serine Endopeptidases; C092897:initiatorin