Purification and characterization of a paralytic polypeptide from larvae of Myrmeleon bore.
A toxic substance was purified from larvae of the antilion, Myrmeleon bore, by DEAE Sephacel and Phenyl Superose column chromatography. The substance was a large polypeptide with a molecular weight of about 165-167 kDa. Its paralytic activity measured by injection against German cockroaches was about 130 times higher than that of tetrodotoxin on a molar basis.
Matsuda
K
K
Department of Agricultural Chemistry, Kinki University, Nara, Japan.
Suzuki
H
H
Nakanishi
F
F
Shio
K
K
Komai
K
K
Nishimura
K
K
D000595:Amino Acid Sequence; D000818:Animals; D001180:Arthropod Venoms / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D003058:Cockroaches / Q000187:drug effects; D007313:Insecta; D007814:Larva / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D013779:Tetrodotoxin / Q000494:pharmacology; D014118:Toxins, Biological / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D014688:Venoms / Q000737:chemistry*
D001180:Arthropod Venoms; D010446:Peptide Fragments; D010455:Peptides; D014118:Toxins, Biological; D014688:Venoms; D013779:Tetrodotoxin