Abstract
In the latent pro-form of matrix metalloproteinase 7 (MMP-7), the cysteine residue in the pro-peptide binds the active-site zinc ion. Hence, recombinant active MMP-7 was prepared from pro-MMP-7 by modification of this cysteine residue with a mercuric reagent. In this study, mature MMP-7 was expressed in Escherichia coli as inclusion bodies, solubilized, and refolded with 1 M L-arginine. The purified product was indistinguishable from the one prepared from pro-MMP-7 as assessed by hydrolysis of (7-methoxycoumarin-4-yl)acetyl-L-Pro-L-Leu-Gly-L-Leu-[N(3)-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl]-L-Ala-L-Arg-NH(2).
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Sequence
-
Arginine / pharmacology
-
Base Sequence
-
Escherichia coli / cytology
-
Escherichia coli / genetics*
-
Gene Expression
-
Humans
-
Hydrogen-Ion Concentration
-
Inclusion Bodies / genetics
-
Matrix Metalloproteinase 7 / biosynthesis*
-
Matrix Metalloproteinase 7 / chemistry
-
Matrix Metalloproteinase 7 / isolation & purification*
-
Matrix Metalloproteinase 7 / metabolism
-
Protein Engineering / methods*
-
Protein Refolding* / drug effects
-
Recombinant Proteins / biosynthesis*
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / isolation & purification*
-
Recombinant Proteins / metabolism
-
Solubility
Substances
-
Recombinant Proteins
-
Arginine
-
Matrix Metalloproteinase 7