Cloning and expression of active domains of human protein disulphide isomerase

1995 ◽  
Vol 23 (1) ◽  
pp. 69S-69S
Author(s):  
STEPHEN H. McLAUGHLIN ◽  
ROBERT B. FREEDMAN
Keyword(s):  
Human Protein ◽  
Cloning And Expression ◽  
Protein Disulphide Isomerase

scholarly journals Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their β subunit

1996 ◽  
Vol 317 (3) ◽  
pp. 721-729 ◽  
Author(s):  
Johanna VEIJOLA ◽  
Pia ANNUNEN ◽  
Peppi KOIVUNEN ◽  
Antony P. PAGE ◽  
Taina PIHLAJANIEMI ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Cloning And Expression ◽  
Β Subunit ◽  
Α Subunit ◽  
Protein Disulphide Isomerase ◽  
C Elegans ◽  
Baculovirus Expression ◽  
Expression Studies ◽  
Α Subunits

Protein disulphide isomerase (PDI; EC 5.3.4.1) is a multifunctional polypeptide that is identical to the β subunit of prolyl 4-hydroxylases. We report here on the cloning and expression of the Caenorhabditis elegans PDI/β polypeptide and its isoform. The overall amino acid sequence identity and similarity between the processed human and C. elegans PDI/β polypeptides are 61% and 85% respectively, and those between the C. elegans PDI/β polypeptide and the PDI isoform 46% and 73%. The isoform differs from the PDI/β and ERp60 polypeptides in that its N-terminal thioredoxin-like domain has an unusual catalytic site sequence -CVHC-. Expression studies in insect cells demonstrated that the C. elegans PDI/β polypeptide forms an active prolyl 4-hydroxylase α2β2 tetramer with the human α subunit and an αβ dimer with the C. elegans α subunit, whereas the C. elegans PDI isoform formed no prolyl 4-hydroxylase with either α subunit. Removal of the 32-residue C-terminal extension from the C. elegans α subunit totally eliminated αβ dimer formation. The C. elegans PDI/β polypeptide formed less prolyl 4-hydroxylase with both the human and C. elegans α subunits than did the human PDI/β polypeptide, being particularly ineffective with the C. elegans α subunit. Experiments with hybrid polypeptides in which the C-terminal regions had been exchanged between the human and C. elegans PDI/β polypeptides indicated that differences in the C-terminal region are one reason, but not the only one, for the differences in prolyl 4-hydroxylase formation between the human and C. elegans PDI/β polypeptides. The catalytic properties of the C. elegans prolyl 4-hydroxylase αβ dimer were very similar to those of the vertebrate type II prolyl 4-hydroxylase tetramer, including the Km for the hydroxylation of long polypeptide substrates.

Expression and secretion of human protein disulphide isomerase in Saccharomyces cerevisiae

1994 ◽  
Vol 22 (1) ◽  
pp. 76S-76S ◽  
Author(s):  
José M. Luz ◽  
H. Markus ◽  
R. Farquhar ◽  
L. D. Schultz ◽  
R. W. Ellis ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Human Protein ◽  
Protein Disulphide Isomerase

scholarly journals 19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b′x from human protein disulphide isomerase (hPDI)

2014 ◽  
Vol 12 (23) ◽  
pp. 3808-3812 ◽  
Author(s):  
Rose Curtis-Marof ◽  
Denisa Doko ◽  
Michelle L. Rowe ◽  
Kirsty L. Richards ◽  
Richard A. Williamson ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Recombinant Protein ◽  
Ligand Binding ◽  
Dissociation Constant ◽  
Human Protein ◽  
19F Nmr ◽  
Protein Disulphide Isomerase ◽  
Protein Labelling ◽  
Nmr Study ◽  
Constant Determination

Fluoroindole recombinant protein labelling enables a 19F NMR study to observe protein–ligand binding and dissociation constant determination.

Cloning and expression of Vibrio cholerae dsbA, a gene encoding a periplasmic protein disulphide isomerase

1995 ◽  
Vol 23 (1) ◽  
pp. 64S-64S ◽  
Author(s):  
EDWARD D. LOWE ◽  
ROBERT B. FREEDMAN ◽  
TIMOTHY R. HIRST ◽  
PETER T. BARTH
Keyword(s):  
Vibrio Cholerae ◽  
Cloning And Expression ◽  
Periplasmic Protein ◽  
Gene Encoding ◽  
Protein Disulphide Isomerase

scholarly journals Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab′ fragment expressed in Escherichia coli

FEBS Letters ◽  
1996 ◽  
Vol 380 (1-2) ◽  
pp. 194-197 ◽  
Author(s):  
David P. Humphreys ◽  
Neil Weir ◽  
Alastair Lawson ◽  
Andrew Mountain ◽  
Peter A. Lund
Keyword(s):  
Escherichia Coli ◽  
Human Protein ◽  
Fab Fragment ◽  
Protein Disulphide Isomerase

scholarly journals Alternative Conformations of the x Region of Human Protein Disulphide-Isomerase Modulate Exposure of the Substrate Binding b’ Domain

2008 ◽  
Vol 383 (5) ◽  
pp. 1144-1155 ◽  
Author(s):  
Van Dat Nguyen ◽  
Katrine Wallis ◽  
Mark J. Howard ◽  
Antti M. Haapalainen ◽  
Kirsi E.H. Salo ◽  
...  
Keyword(s):  
Substrate Binding ◽  
Human Protein ◽  
Protein Disulphide Isomerase
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