Molecular characterization of the bifunctional VHDL-CP from the hemolymph of white shrimp Penaeus vannamei.
A very high-density lipoprotein (VHDL) purified from the hemolymph of the white shrimp Penaeus vannamei is shown to be identical to the clotting protein (CP) previously reported from the same organism based on size, subunits and N-terminal amino acid sequence. The approximately 440-kDa protein, a homodimer of approximately 200-kDa subunits, was present in KBr gradient fractions ranging in density from 1.155 to 1.212 g/ml. Samples of VHDL after purification by strong cation exchange chromatography were subjected to electrophoresis on native polyacrylamide gels. Lipids associated with the VHDL were detected by Sudan Black and Oil Red O staining and comprise 9-15% of the purified protein. Circular dichroism of VHDL-CP indicates that the alpha-helix content of the VHDL-CP is 32%, while beta-sheets correspond to 33%, closely resembling the secondary structure of CP from the shrimp Penaeus monodon and, remarkably, the secondary structure of very high-density lipophorin E (VHDLpE) from the tobacco hornworm, Manduca sexta.
Yepiz-Plascencia
Gloria
G
Marine Biotechnology, Centro de Investigación en Alimentación y Desarrollo, P.O. Box 1735, Sonora 83000, Hermosillo, Mexico. gyepiz@cascabel.ciad.mx
Jiménez-Vega
Florinda
F
Romo-Figueroa
María Gabriela
MG
Sotelo-Mundo
Rogerio R
RR
Vargas-Albores
Francisco
F
D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D006458:Hemolymph / Q000737:chemistry*; D008075:Lipoproteins, HDL / Q000737:chemistry* / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D033561:Penaeidae / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D008075:Lipoproteins, HDL; C026277:very high density lipoproteins