A male accessory gland peptide with protease inhibitory activity in Drosophila funebris.
Male accessory glands of Drosophila funebris synthesize and secrete a peptide that shows a protease-inhibiting activity. Amino acid sequencing of the purified peptide revealed that the peptide consists of 63 amino acid residues. It is a serine protease inhibitor belonging to the pancreatic trypsin inhibitor (Kunitz) family. The inhibitory function and the kinetic characteristics of the inhibition have been examined with various substrates. The peptide possibly plays a role as an acrosin inhibitor involved in Drosophila reproduction.
Schmidt
T
T
Zoology Institute, University of Zurich, Switzerland.
Stumm-Zollinger
E
E
Chen
P S
PS
Böhlen
P
P
Stone
S R
SR
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004330:Drosophila / Q000378:metabolism*; D005837:Genitalia, Male / Q000378:metabolism; D007700:Kinetics; D008297:Male; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D011480:Protease Inhibitors / Q000235:genetics / Q000302:isolation & purification* / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism
D010446:Peptide Fragments; D011480:Protease Inhibitors; D014357:Trypsin