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. 1989 May 1;259(3):627–631. doi: 10.1042/bj2590627

Lactoperoxidase from human colostrum.

B Langbakk 1, T Flatmark 1
PMCID: PMC1138564  PMID: 2658975

Abstract

The present study has confirmed that human colostrum contains a lactoperoxidase (EC 1.11.1.7) [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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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