Add time:09/02/2019         Source:sciencedirect.com

The ability of hematin (4·9 μm) to catalyze oxidation of a linoleate emulsion in dimethyl arsenic acid buffer, pH 7·4, was tested as a function of calcium (20 mm), β-casein (250 μm) and temperature (7°–25°C). A polarographic oxygen sensor was used to monitor reaction rates. In all samples, a fairly similar pattern of increase in rate was observed with increasing temperature. The presence of β-casein, a protein that exhibits aggregation above 4°C and calcium-induced precipitation at about 20°C, was expected to cause an unusual temperature-dependence, but this was not observed. β-casein did, however, cause substantial inhibition of hematin-catalyzed oxidation at all temperatures above 7°C when calcium was absent. This is likely to be attributable to hydrophobic association between β-casein and hematin or molecular encapsulation of linoleate by β-casein. Calcium was inhibitory at 20·5° and 26°C when β-casein was absent.

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