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 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.
Langbakk
B
B
Department of Biochemistry, University of Bergen, Norway.
Flatmark
T
T
D002846:Chromatography, Affinity; D002851:Chromatography, High Pressure Liquid; D003126:Colostrum / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006801:Humans; D007163:Immunosorbent Techniques; D007784:Lactoperoxidase / Q000302:isolation & purification*; D010544:Peroxidases / Q000302:isolation & purification*; D011247:Pregnancy; D011863:Radioimmunoassay
D007784:Lactoperoxidase; D010544:Peroxidases