Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P04155 (
pS2
)
1,234
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The preparation and purification of recombinant mature
pNR-2
/
pS2
, a single-domain member of the 'trefoil' family of cysteine-rich secreted proteins, is described. Analysis of recombinant
pNR-2
/
pS2
by ion-exchange chromatography showed that it was heterogeneous. The heterogeneity was reduced by treatment with thiol-group-containing reagents, suggesting that it is caused by the odd number of cysteine residues in mature
pNR-2
/
pS2
, and this view was reinforced by mutation of the extra-trefoil domain cysteine residue, Cys58, to a serine residue. Electrophoresis of recombinant
pNR-2
/
pS2
Cys58 and
pNR-2
/
pS2
Ser58 proteins under non-denaturing conditions confirmed that the Ser58 mutant is much more homogeneous, and showed that most of
pNR-2
/
pS2
Ser58 co-migrates as a single band with
pNR-2
/
pS2
secreted from breast-cancer cells in culture. Treatment of recombinant
pNR-2
/
pS2
proteins with various thiol-group-reactive reagents indicated that cysteine is the most effective at producing recombinant
pNR-2
/
pS2
that co-migrates with
pNR-2
/
pS2
secreted by breast-cancer cells.
Dithiothreitol
appeared to denature the proteins, and GSH was relatively ineffective.
pNR-2
/
pS2
Cys58 treated with cysteine and untreated
pNR-2
/
pS2
Ser58 had the same apparent molecular mass, measured by gel filtration, as
pNR-2
/
pS2
secreted from breast-cancer cells. This is the first report of the production of a recombinant mature single-domain trefoil peptide and should greatly facilitate elucidation of the structure and function of
pNR-2
/
pS2
.
...
PMID:Production and comparison of mature single-domain 'trefoil' peptides pNR-2/pS2 Cys58 and pNR-2/pS2 Ser58. 894 62
