Open AccessThe Amino‐Acid Sequence of a Peptide (PS‐1) from Drosophila funebris: A Paragonial Peptide from Males which Reduces the Receptivity of the Female
Author(s) -
BAUMANN Heinz,
WILSON Kenneth J.,
CHEN Pei Shen,
HUMBEL René E.
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb04023.x
Subject(s) - receptivity , peptide , drosophila (subgenus) , peptide sequence , biology , genetics , endocrinology , biochemistry , gene
The substance, PS‐1, produced in the paragonial gland of adult male Drosophila funebris influences the mating behavior of virgin female flies after injection. The substance was isolated and characterized as a 27‐residue peptide. The complete amino acid sequence was determined by manual sequence analysis of tryptic peptides, automated Edman degradation, and carboxypeptidase A digestion. The sequence is Asp‐ Val Leu ‐Pro‐Ser‐Ala‐Asn‐Ala‐Asn‐Ala‐Asn‐Asn‐Gln‐Arg‐Thr‐Ala‐Ala‐Ala‐Lys‐Pro‐Gln‐Ala‐Asn‐Ala‐Glu‐Ala‐Ser‐Ser. The ratio of Val: Leu in the second position of the sequence is 7:3. This is the first detailed report on an insect peptide which causes a biological response in the opposite sex following mating.