Biochemical and proteomic characterisation of haemolymph serum reveals the origin of the alkali-labile phosphate (ALP) in mussel (Mytilus galloprovincialis)

摘要: Mollusc haemolymph proteins are known to play several important physiological roles in the immune system, heavy metal transport and tissue distribution of lipophilic compounds. In this study, we analysed acetone-extracted from mussel by one- two-dimensional gel electrophoresis. The were identified comparing mass spectrometry data with invertebrate EST database, allowing us establish serum proteome. Extrapallial protein (EP) precursor represents most abundant protein; astacin CuZn superoxide dismutase also detected. Slight contamination muscle proteins, due sampling method, was found. No differences observed profiles obtained for male female proteins. One aspect interest previously reported finding that alkali-labile phosphate (ALP) may be representative vitellogenin (vtg)-like content circulatory fluid molluscs. our analysis serum, vitellogenin-like never To confirm these data, a typical methyl-tert-butyl-ether (MTBE) extraction, which is specific vtg-like performed, results electrophoretic analyses compared those acetonic precipitation. showed similar cannot identified. Moreover, main phosphoprotein present extracts EP precursor. addition, agarose electrophoresis demonstrates high-molecular-weight forms not detectable.