Demonstration and partial purification of lactoperoxidase from human colostrum.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Langbakk B,Flatmark T

doi

10.1016/0014-5793(84)81177-1

subject

Has Abstract

pub_date

1984-09-03 00:00:00

pages

300-3

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(84)81177-1

journal_volume

174

pub_type

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