Pyruvate dehydrogenase of rat mammary tissue showed many of the regulatory properties of the analogous enzyme in other mammalian tissues. It was inactivated in the presence of low concentrations of ATP and this rate of inactivation was slowed if pyruvate or PP1 was also present. Reactivation by Mg2+ in the presence of low concentrations of Ca2+ occurred over a similar time-course. The Km value for Mg2+ in this process was about 2mm. The enzyme was assayed in extracts of freeze-clamped mammary glands removed from pregnant, lactating or recently weaned rats under halothane anaesthesia. Both the initial activity and the activity after full activation (‘total enzyme activity’) were determined. The former parameter, when expressed on a DNA basis, varied within a range of 40 times its lowest value. Maximum total enzyme activity was about 1 unit/g wet wt. The total enzyme activity and the fraction in the active form increased in step from pregnancy to mid-lactation, remained elevated until the end of lactation and then fell steeply within 3 days after weaning. The correlation of these two parameters of enzyme activity may indicate a common regulatory factor or else an interdependence arising from inherent properties of the multi-enzyme complex.

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