Demonstration and partial purification of lactoperoxidase from human colostrum

A peroxidase with stability, chromatographic and immunoreactive properties similar to that of bovine lactoperoxidase has been partly purified from human colostrum. Hydrophobic interaction chromatography on Phenyl-Sepharose C1–4B gave a 10-fold purification with an apparent recovery of about 45%. The...

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Bibliographic Details
Published in:FEBS letters 1984-09, Vol.174 (2), p.300-303
Main Authors: Langbakk, Bodil, Flatmark, Torgeir
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Chromatography, Affinity
colostrum
Colostrum - enzymology
Enzymes and enzyme inhibitors
Eosinophils - enzymology
Epitopes - immunology
Fundamental and applied biological sciences. Psychology
Humans
Immunosorbent Techniques
Isoenzymes - immunology
lactoperoxidase
Lactoperoxidase - immunology
Lactoperoxidase - isolation & purification
Leukocytes - enzymology
man
Oxidoreductases
Peroxidase - immunology
Peroxidases - immunology
Peroxidases - isolation & purification
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Summary:A peroxidase with stability, chromatographic and immunoreactive properties similar to that of bovine lactoperoxidase has been partly purified from human colostrum. Hydrophobic interaction chromatography on Phenyl-Sepharose C1–4B gave a 10-fold purification with an apparent recovery of about 45%. The enzyme was quantitatively and specifically adsorbed to beads of anti-lactoperoxidase (bovine)-Protein A-Sepharose. No adsorption of the enzyme was observed on immunoadsorbent columns prepared with high-titre polyclonal antibodies raised against human myeloperoxidase and human eosinophile peroxidase. Lactoperoxidase Human colostrum Protein A-Sepharose Myeloperoxidase Eosinophile peroxidase
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(84)81177-1