Purification and characterization of biliverdin-binding protein from larval hemolymph of the swallowtail butterfly, Papilio xuthus L.
The biliverdin-binding protein from the larval hemolymph of the swallowtail butterfly, Papilio xuthus L., was purified and characterized. The crude biliverdin-binding protein, obtained by ammonium sulfate fractionation, was purified in two steps, the first one by gel filtration chromatography and the second one by ion-exchange chromatography. The molecular mass of the purified protein was analyzed by SDS-polyacrylamide gel electrophoresis and estimated to be 21 kDa. The Namino terminal sequence of P. xuthus biliverdin-binding protein analyzed up to the 19th residue showed that 42% of the amino acid sequence are sequence similarity to the bilin-binding protein from Pieris brassicae. These results suggest that the P. xuthus biliverdin-binding protein belongs to the insecticyanin-type.
Yamanaka
A
A
Department of Physics, Biology and Informatics, Faculty of Science, Yamaguchi University, Japan. yamanaka@po.cc.yamaguchi-u.ac.jp
Ito
T
T
Koga
D
D
Sato
T
T
Ochiai
M
M
Endo
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001664:Biliverdine / Q000378:metabolism; D002080:Butterflies; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006458:Hemolymph / Q000737:chemistry*; D019476:Insect Proteins; D007447:Invertebrate Hormones / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D007814:Larva; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D000596:Amino Acids; D002352:Carrier Proteins; D019476:Insect Proteins; D007447:Invertebrate Hormones; C043409:insecticyanin protein, insect; D001664:Biliverdine