Crystalline Horse Liver Catalase

Dounce, Alexander L.; Frampton, Orville D.

doi:10.1126/science.89.2309.300

Cited by 21 publications

(1 citation statement)

References 1 publication

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In order to purify the enzyme, a new, simplified method is required. The catalase enzyme is distributed widely in animals (Dounce and Frampton, 1939;Deisseroth and Dounce, 1969;Sarkar and Sumner, 1951;Sumner and Dounce, 1937) and plants (Schiefer et al, 1976), including microorganisms (Herbert and Pinsent, 1947;Kamel and Tahany, 1973) and is said to have common antigens (Higashi et al, 1965). Thus, an anti-catalase serum produced from the catalase of a given animal should cross-react with catalase from other species to precipitate.…”

Section: Introductionmentioning

confidence: 99%

Purification of Milk Catalase by Immunoaffinity Chromatography

Ito

Kamata

Kakiichi

et al. 1990

Journal of Food Science

View full text Add to dashboard Cite

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 × 104 times as pure as cows' milk. The purified catalase was electrophoretically homogeneous, appearing as a single band.

show abstract