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Efficient production of native, biologically active human cystatin C by Escherichia coli

In English

Författare

Summary, in English

A cDNA encoding the mature human cysteine proteinase inhibitor cystatin C was fused to the coding sequence for the Escherichia coli outer membrane protein A signal peptide, and the recombinant gene was expressed in E. coli under the control of the λ PR promoter, an optimized Shine-Dalgarno sequence and the λ cI 857 repressor. When induced at 42°C, such cells expressed large amounts of recombinant cystatin C. The recombinant protein was isolated in high yield and characterized. All physicochemical properties investigated, including the positions of disulfide bonds, indicated that the E. coli derived cystatin C was identical to cystatin C isolated from human biological fluids, except that the proline residue in position three was not hydroxylated. The recombinant protein displayed full biological activity against papain, cathepsin B and dipeptidyl peptidase I.

Publiceringsår

1988

Språk

Engelska

Sidor

14-18

Publikation/Tidskrift/Serie

FEBS Letters

Volym

236

Issue

1

Dokumenttyp

Artikel i tidskrift

Förlag

Wiley-Blackwell

Ämne

  • Biological Sciences

Nyckelord

  • Cystatin C
  • Cysteine proteinase inhibitor
  • Gene expression
  • Amyloidosis
  • Cerebral hemorrhage

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1873-3468