The present study has confirmed that human colostrum contains a lactoperoxidase (EC 18.104.22.168) [Langbakk & Flatmark (1984) FEBS Lett. 174, 300-303], which represents about 0.004% of the total protein in crude colostrum. An apparent 32-fold purification of the enzyme was obtained by a multistep procedure, as modified from that of the bovine enzyme, with a recovery of about 7%. By use of chromatography on an immunoaffinity column (directed against bovine lactoperoxidase B), an apparent 1450-fold purification was obtained in a single step, with a recovery of 21%. The enzyme behaved as a glycoprotein (binding to concanavalin A-Sepharose), and revealed spectral properties (Soret peak at 412 nm) and an Mr (80,000) similar to those of the bovine enzyme.
Research Article|May 01 1989
Lactoperoxidase from human colostrum
Biochem J (1989) 259 (3): 627-631.
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B Langbakk, T Flatmark; Lactoperoxidase from human colostrum. Biochem J 1 May 1989; 259 (3): 627–631. doi: https://doi.org/10.1042/bj2590627
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