Isolation and characterization of an apoptosis-inhibiting component from the hemolymph of Bombyx mori.
Silkworm (Bombyx mori) hemolymph showed an apoptosis-inhibiting activity in insect cells (Sf 9) infected with baculovirus (AcNPV). The addition of silkworm hemolymph into the culture medium increased the host cell longevity due to its apoptosis-inhibition activity. Components with an apoptosis-inhibiting effect were purified from the silkworm hemolymph by heat treatment, gel-filtration chromatography, and ion-exchange chromatography. The component with highest activity was characterized by periodic acid-Schiff staining, isoelectric focusing, MALDI-TOF-mass spectrometry, and N-terminal sequencing and was found to be a nonglycosylated monomeric protein with a molecular weight of ca. 28,000 Da.
Kim
E J
EJ
School of Chemical Engineering, Seoul National University, Kwanak-Gu Shilim-Dong San 56-1, Seoul 151-744, Korea.
Rhee
W J
WJ
Park
T H
TH
D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis / Q000187:drug effects / Q000502:physiology*; D016367:Baculoviridae; D012831:Bombyx; D002460:Cell Line; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003470:Culture Media; D006458:Hemolymph / Q000737:chemistry / Q000502:physiology*; D019476:Insect Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D018411:Spodoptera; D014162:Transfection
D003470:Culture Media; D019476:Insect Proteins; D010446:Peptide Fragments