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 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.
D002846:Chromatography, Affinity; D003126:Colostrum / Q000201:enzymology*; D004804:Eosinophils / Q000201:enzymology; D000939:Epitopes / Q000276:immunology; D006801:Humans; D007163:Immunosorbent Techniques; D007527:Isoenzymes / Q000276:immunology; D007784:Lactoperoxidase / Q000276:immunology / Q000302:isolation & purification*; D007962:Leukocytes / Q000201:enzymology; D009195:Peroxidase / Q000276:immunology; D010544:Peroxidases / Q000276:immunology / Q000302:isolation & purification*
D000939:Epitopes; D007527:Isoenzymes; D007784:Lactoperoxidase; D010544:Peroxidases; D009195:Peroxidase