Marco Fragai - Profile on Academia.edu (original) (raw)

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Papers by Marco Fragai

Research paper thumbnail of Expression and high yield production of the catalytic domain of matrix metalloproteinase 12 and of an active mutant with increased solubility

Journal of Molecular Catalysis A: Chemical, 2003

In the general frame of a project aiming at screening candidate drugs against several different m... more In the general frame of a project aiming at screening candidate drugs against several different matrix metalloproteinases (MMP) to find a rationale for selectivity, the catalytic domain of MMP-12 (metalloelastase) has been expressed in E. coli strain BL21D3 and its production optimized to about 30 mg/dm 3 . The chosen construct spans residues 106-267 of the whole MMP-12 and contains two additional methionines at positions 104-105. This is at variance with the previously published constructs which span residues 99-279 [J. Mol. Biol. 312 743] and 100-262 [J. Mol. Biol. 312 (2001) 731], respectively.

Research paper thumbnail of Expression and high yield production of the catalytic domain of matrix metalloproteinase 12 and of an active mutant with increased solubility

Journal of Molecular Catalysis A: Chemical, 2003

In the general frame of a project aiming at screening candidate drugs against several different m... more In the general frame of a project aiming at screening candidate drugs against several different matrix metalloproteinases (MMP) to find a rationale for selectivity, the catalytic domain of MMP-12 (metalloelastase) has been expressed in E. coli strain BL21D3 and its production optimized to about 30 mg/dm 3 . The chosen construct spans residues 106-267 of the whole MMP-12 and contains two additional methionines at positions 104-105. This is at variance with the previously published constructs which span residues 99-279 [J. Mol. Biol. 312 743] and 100-262 [J. Mol. Biol. 312 (2001) 731], respectively.

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