0000000000164521

AUTHOR

Patrick J. Walsh

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Isolation and characterization of haemoporin, an abundant haemolymph protein from Aplysia californica.

2003

In the present study, we show the isolation and characterization of the protein haemoporin, which constitutes the second most abundant protein fraction in the haemolymph of the marine gastropod Aplysia californica. Although Aplysia is commonly used to investigate the molecular basis of learning, not much is known about the proteins in its haemolymph, which is in contact with the neurons owing to the open circulatory system of molluscs. In the native state, haemoporin is a macromolecular complex forming a cylinder with a central solvent-filled pore. The native complex most probably is a homopentamer made up from 70 kDa subunits with a molecular mass of 360 kDa and a sedimentation coefficient…

Circular dichroismanimal structuresMolecular Sequence DataMegathura crenulataBiochemistrySequence Analysis ProteinHemolymphHemolymphAplysiaNative stateAnimalsAmino Acid SequenceMolecular BiologyProtein secondary structurebiologyMolecular massCircular DichroismCell BiologyAnatomyBlood Proteinsbiology.organism_classificationMolecular WeightMicroscopy ElectronSpectrometry FluorescenceBiochemistryAplysiaProtein quaternary structureElectrophoresis Polyacrylamide GelUltracentrifugationResearch ArticleThe Biochemical journal
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