Expression and characterization of the intact N-terminal domain of streptokinase.
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.
Oxford Centre for Molecular Sciences and New Chemistry Laboratory, University of Oxford, United Kingdom.
A I
AI
Azuaga
N D
ND
Woodruff
F
F
Conejero-Lara
V F
VF
Cox
R A
RA
Smith
C M
CM
Dobson
D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D004926:Escherichia coli / Q000737:chemistry; D002479:Inclusion Bodies / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D017434:Protein Structure, Tertiary; D013300:Streptokinase / Q000378:metabolism*; D013696:Temperature; D014170:Transformation, Genetic
D013300:Streptokinase