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Purification of Milk Catalase by Immunoaffinity Chromatography
Author(s) -
ITO O.,
KAMATA S.,
KAKIICHI N.,
SUZUKI Y.,
HAYASHI M.,
UCHIDA K.
Publication year - 1990
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1990.tb01627.x
Subject(s) - catalase , chemistry , chromatography , antiserum , cyanogen bromide , affinity chromatography , sepharose , cyanogen , homogeneous , ammonium sulfate , high performance liquid chromatography , biochemistry , antibody , enzyme , biology , peptide sequence , organic chemistry , thermodynamics , physics , gene , immunology
Antiserum against commercially available bovine liver catalase was prepared in rabbits. Anti‐catalase antibody in serum was prepared following 30% ammonium sulfate treatment and Sephacryl S‐300 column chromatography. The anti‐catalase antibody was coupled to cyanogen bromide‐activated Sepharose 4B, and using this immunoadsorbent crude milk catalase was purified. About 7.0 mg pure catalase was produced from 10 kg milk. Activity of the purified products was about 2.58 × 10 4 times as pure as cows' milk. The purified catalase was electrophoretically homogeneous, appearing as a single band.