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Analysis of recombinant human saposin A expressed by Pichia pastoris.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Yamada M,Inui K,Hamada D,Nakahira K,Yanagihara K,Sakai N,Nishigaki T,Ozono K,Yanagihara I

doi

10.1016/j.bbrc.2004.04.069

subject

Has Abstract

pub_date

2004-05-28 00:00:00

pages

588-93

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X04007910

journal_volume

318

pub_type

杂志文章

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