Hostname: page-component-848d4c4894-m9kch Total loading time: 0 Render date: 2024-06-01T08:20:41.072Z Has data issue: false hasContentIssue false
  • English
  • Français

Expression and characterization of the intact N-terminal domain of streptokinase

Published online by Cambridge University Press:  01 February 1999

ANA I. AZUAGA ,
NICHOLAS D. WOODRUFF ,
FRANCISCO CONEJERO-LARA ,
VIVIENNE F. COX ,
RICHARD A.G. SMITH  and
CHRISTOPHER M. DOBSON
ANA I. AZUAGA
Affiliation:
Oxford Centre for Molecular Sciences and New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, United Kingdom Departamento de Química Física, Facultad de Ciencias, e Instituto de Biotecnología, Universidad de Granada, 18071 Granada, Spain
NICHOLAS D. WOODRUFF
Affiliation:
Oxford Centre for Molecular Sciences and New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, United Kingdom
FRANCISCO CONEJERO-LARA
Affiliation:
Departamento de Química Física, Facultad de Ciencias, e Instituto de Biotecnología, Universidad de Granada, 18071 Granada, Spain
VIVIENNE F. COX
Affiliation:
AdProTech plc., Unit 3, 2 Orchard Road, Royston, Herts., SG8 5HD, United Kingdom
RICHARD A.G. SMITH
Affiliation:
AdProTech plc., Unit 3, 2 Orchard Road, Royston, Herts., SG8 5HD, United Kingdom
CHRISTOPHER M. DOBSON
Affiliation:
Oxford Centre for Molecular Sciences and New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, United Kingdom
Get access

Abstract

Proteolytic studies have enabled two of the three putative domains of the fibrinolytic protein streptokinase to be isolated and characterized (Conejero-Lara F et al., 1996, Protein Sci 5:2583–2591). The N-terminal domain, however, could not be isolated in these experiments because of its susceptibility to proteolytic cleavage. To complete the biophysical characterization of the domain structure of streptokinase we have overexpressed, purified, and characterized the N-terminal region of the protein, residues 1–146. The results show this is cooperatively folded with secondary structure content and overall stability closely similar to those of the equivalent region in the intact protein.

Keywords

biophysical characterizationfibrinolytic proteinstreptokinaseisolationthermal stability
Type
FOR THE RECORD
Information
Protein Science , Volume 8 , Issue 2 , February 1999 , pp. 443 - 446
Copyright
© 1999 The Protein Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)