[Purification of a Storage Protein from Aphis craccivora Koch and Its Subunit Characterization].
By using of DE52 Cellulose, Sephadex G-150 and FPLC Q Sepharose chromatography, a storage protein (SP) was purified from Aphis craccivora Koch and its subunit was characterized. Its molecular weight was about 60 kD as determined by SDS-PAGE analysis under both reducing and non-reducing conditions, and its pI was about 5.0. It was a glycoprotein. The protein accumulated in larval hemolymph, and decreased when host turned to adult, and could be detected in adults in very low concentration. According to the molecular weight, amino acids composition, and its dynamic alteration of concentrations, the protein should be a persisting storage protein of hemimetabolous insects.
Gan
Ming
M
Institute of Plant Physiology and Ecology, Shaghai Institutes for Biomedical Sciences, the Chinese Academy of Sciences, Shanghai 200032, China.
Ding
De-Cheng
DC
Zhou
Yuan-Cong
YC
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001042:Aphids / Q000737:chemistry*; D002241:Carbohydrates / Q000032:analysis; D002845:Chromatography / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D006458:Hemolymph / Q000737:chemistry; D019476:Insect Proteins / Q000737:chemistry / Q000302:isolation & purification*; D008055:Lipids / Q000032:analysis; D021122:Protein Subunits / Q000737:chemistry / Q000302:isolation & purification
D000596:Amino Acids; D002241:Carbohydrates; D019476:Insect Proteins; D008055:Lipids; D021122:Protein Subunits; C041137:storage proteins, Insecta