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Purification and characterization of three major hemolymph proteins of an insect, Calpodes ethlius (lepidoptera, hesperiidae)
Author(s) -
Palli Subba Reddy,
Locke Michael
Publication year - 1987
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940050403
Subject(s) - hemolymph , lepidoptera genitalia , polyacrylamide gel electrophoresis , biology , random hexamer , gel electrophoresis , protein subunit , sodium dodecyl sulfate , biochemistry , glycine , storage protein , amino acid , botany , enzyme , gene
Like many other Lepidoptera, fifth‐stage Calpodes larvae have three major hemolymph proteins. Their molecular weights were estimated by 3‐15% nondenaturing polyacrylamide gel electrophoresis (N‐PAGE) as 470,000 (arylphorin; Ar), 580,000 (storage protein 2; SP2) and 720,000 (storage protein 1; SP1). Carbohydrate is associated with all three, but only Ar has lipid. The three proteins have been purified by preparative N‐PAGE and sodium dodecyl sulfate (SDS)‐polyacrylamide gel electrophoresis. On 3‐15% SDS gels, Ar dissociated into 82,000 M r subunits, SP2 into 86,000 M r subunits, and SP1 into both 86,000 and 90,000 M r subunits. The 470,000 M r protein is identified as Ar because it is rich in aromatic amino acids. The 580,000 and 720,000 M r proteins are rich in glycine and are called storage proteins. Electron microscopy of negatively stained preparations shows that each polymer has a different geometrical arrangement of subunits. SP1 is a cube made from eight subunits. SP2 is a hexamer in the form of a pentahedral prism. Ar is probably an octahedron made from six subunits. All three geometrical arrangements could permit the presence of a central carrying space.