Lactoperoxidase folding and catalysis relies on the stabilization of the α-helix rich core domain: A thermal unfolding study

Author:

Boscolo Barbara,Leal Sónia S.,Ghibaudi Elena M.,Gomes Cláudio M.

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference53 articles.

1. Lactoperoxidase: physico-chemical properties, occurrence, mechanism of action and applications;Kussendrager;Br. J. Nutr.,2000

2. Heme peroxidases;Dunford,1999

3. The gene encoding lactoperoxidase is expressed in epithelial cells of the goat lactating mammary gland;Cals;Cell. Mol. Biol. (Noisy-le-grand),1994

4. Antibacterial activity of the lactoperoxidase system — a review;Wolfson;J. Food Prot.,1993

5. Determination of the carbohydrate composition and the disulfide bond linkages of bovine lactoperoxidase by mass spectrometry;Wolf;J. Mass Spectrom.,2000

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