By P.B. Bradley and R.W. Brimblecombe (Eds.)
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Additional info for Biochemical and Pharmacological Mechanisms Underlying Behaviour
Isoelectric focusing experiments The molecular heterogeneity of ChAc from different species was further investigated by isoelectric focusing of partially purified enzyme preparations. 75 W for the pH gradient 6-9. Constant current was usually obtained after 36 h but the column was stopped after 46 h. 1 (Fig. 5a). The peak of enzyme activity did not change on re-focusing in a second gradient nor was the peak changed by the presence of 3 M urea to decrease any glass wall effects or protein-enzyme interactions.
Isoelectric focusing of A, ChAc from pigeon brain; and B, ChAc from guinea-pig brain in pH gradient 3-10. ) pH. In contrast to the enzymes from pigeon and guinea-pig brains the enzymes from rat and cat brains were distributed over a rather broader pH range. 3 in a pH 3-10 gradient (Fig. 6a). The identity of two separate peaks was established by isolating the most active fractions in the two peaks and re-focusing them in two separate pH 6-9 gradients (Fig. 6b). The results showed that the two new peaks did not overlap and therefore corresponded to two or more different forms of the enzyme.
The identity of two separate peaks was established by isolating the most active fractions in the two peaks and re-focusing them in two separate pH 6-9 gradients (Fig. 6b). The results showed that the two new peaks did not overlap and therefore corresponded to two or more different forms of the enzyme. 3 (Fig. 6c). The necessity of re-focusing experiments was demonstrated with an extract of enzyme from rat caudate nuclei. 0. 3. This peak is therefore probably an artifact resulting from protein-enzyme interaction.
Biochemical and Pharmacological Mechanisms Underlying Behaviour by P.B. Bradley and R.W. Brimblecombe (Eds.)