Lactoperoxidase from human colostrum

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 pr...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical journal 1989-05, Vol.259 (3), p.627-631
Main Authors: Langbakk, B, Flatmark, T
Format: Article
Language:English
Subjects:
Chromatography, Affinity
Chromatography, High Pressure Liquid
colostrum
Colostrum - enzymology
Electrophoresis, Polyacrylamide Gel
Female
Humans
Immunosorbent Techniques
Lactoperoxidase - isolation & purification
man
Peroxidases - isolation & purification
Pregnancy
Radioimmunoassay
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2590627