[Carbon dioxide fixation by aspartic acid and the influence of biotin on this fixation].
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Bilateral application of N-methyl-D-aspartate (NMDA) and kainic acid to the substantia nigra, pars compacta (SNc) and the ventral tegmental area (VTA) induced enhanced motor responses in the rat. A greater locomotor response was elicited from the VTA; sniffing was also observed following SNc injections. Both motor activities were blocked by systemic fluphenazine. Application of NMDA and kainate to the substantia nigra pars reticulata caused sedation and catalepsy. The experiments illustrate a dual motor response for excitatory amino acids when applied to either pars compacta or pars reticulata of the rat SN.
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The effects of mutation of residue Ala-128 of the b subunit of Escherichia coli ATP synthase to aspartate on the structure of the subunit and its interaction with the F(1) sector were analyzed. Determination of solution molecular weights by sedimentation equilibrium ultracentrifugation revealed that the A128D mutation had little effect on dimerization in the soluble b construct, b(34-156). However, the mutation caused a structural perturbation detected through both a 12% reduction in the sedimentation coefficient and also a reduced tendency to form intersubunit disulfide bonds between cysteine residues inserted at position 132. Unlike the wild-type sequence, the A128D mutant was unable to interact with F(1)-ATPase. These results indicate that the A128D mutation caused a structural change in the C-terminal region of the protein, preventing the binding to F(1) but having little or no effect on the dimeric nature of b.