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Inter- and intramolecular domain interactions of the catalase-peroxidase KatG from M. tuberculosis.

FEBS letters (2001-12-14)
M Wilming, K Johnsson
ABSTRACT

The inter- and intramolecular interactions between the different domains of the catalase-peroxidase KatG from Mycobacterium tuberculosis were analyzed using the two-hybrid assay. It was shown that the dimerization of the enzyme is due to a strong interaction of the first 99 amino acids of the N-terminal domain whereas the C-terminal domain does not play a role in the dimerization. In addition, an intramolecular interaction between the N- and C-terminal domains was detected which might play a functional role in the mechanism of the enzyme.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Mouse IgG (whole molecule)–Peroxidase antibody produced in goat, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
Anti-Rabbit IgG (whole molecule)–Peroxidase antibody produced in goat, affinity isolated antibody, buffered aqueous solution