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  • Title: Analysis of recombinant human saposin A expressed by Pichia pastoris.
    Author: Yamada M, Inui K, Hamada D, Nakahira K, Yanagihara K, Sakai N, Nishigaki T, Ozono K, Yanagihara I.
    Journal: Biochem Biophys Res Commun; 2004 May 28; 318(2):588-93. PubMed ID: 15120640.
    Abstract:
    Saposins (SAPs) are small glycoproteins required for activation of sphingolipid hydrolysis by lysosomal enzymes. Four SAPs, SAP-A, -B, -C, and -D, are proteolytically cleaved from a single gene product termed prosaposin. The mature coding sequence of human SAP-A tagged with 6-histidine was expressed in Pichia pastoris and the recombinant protein was purified from the culture supernatant by simple purification steps with an immobilized metal ion affinity column, a Concanavalin A column, and reversed-phase HPLC. Secreted SAP-A contained both glycosylated and nonglycosylated forms. Both forms of SAP-A activated galactocerebroside and 4-methylumbelliferyl beta-d-glucoside hydrolysis by galactocerebrosidase and glucocerebrosidase. SAP-A expressed in P. pastoris should be useful for further structural and functional analysis of this protein.
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