By W. N. Aldridge (eds.)

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2. A tail response can be evoked in the rat by slowly raising the body temperature above the set point for heat release (SPHR). This was done with the aid of radiant heat from incandescent lamps. Recent experiments (Meeter, 1969) showed that following an injection of a suitable dose of an anti-ChE, the SPHR is drastically lowered, and then gradually regains its normal level during the subsequent hours. Fig. 4 illustrates an experiment in which a small amount of soman was injected intraventricularly with the aid of a guide-tube placed through the skull on the previous day.

Gass, & S. L. N. Rao CAF} AMP H 8 0 4 1E c 14 14 ATP ·I e X {3·84 nmol ( 32 P) 434 nmol ( 14 C) 1- - 2 11- ·I ADP .... Origin M 4 I I 8 I 4·16nmol lr-f" 1 12 16 L I 20 I l I 24 em FIG. 10. Separation of radioactive compounds obtained after denaturation of the inhibited enzyme. A mixture (vol. /nmol phosphate), KCl (0·1 M), imidazole-HCl buffer, pH 7·2 (0·01 M), EDTA (0·1 mM) was incubated for 30 min at 37°C; enzymatic activity was completely inhibited. The solution was added to a column of Sephadex G-50 (0·8 x 18 em) previously equilibrated with NH 4 HC0 3 (pH 8·0; 0·05 M) and 0·1 mM EDTA.

O- and L-glutamic acid; the hydrogen atoms that are encircled and indicated by arrows may be substituted by methyl groups without loss of enzymatic susceptibility. Glutamine Synthetase Inhibition H2N r'l 47 H2N HOOC~COOH HOOC~COOH L- cis -1-Amino-1 ,3dicarboxycyclohexane L-glutamic acid FIG. 5. L-Glutamic acid and L-cis-1-amino-1,3-dicarboxycyclohexane. synthetase, is a good substrate provides strong evidence for the hypothesis that L-glutamic acid is attached to the active site of the enzyme in the extended conformation as originally postulated.

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A Symposium on Mechanisms of Toxicity by W. N. Aldridge (eds.)
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