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Download Chemical and Molecular Basis of Nerve Activity by David Nachmansohn PDF

By David Nachmansohn

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CONDUCTION AND ACTIVITY OF ACETYLCHOLINESTERASE was demonstrated in the following way. If ν is the reaction velocity in the absence of the inhibitor I, and t/ in its presence, and ν/υ' is plotted against the concentration of the inhibitor, a straight line is obtained in the case of competitive inhibition at constant concentrations of enzyme according to the equation: - 1 + Kj([S] m + K) S [S] and [7] are the concentrations of substrate and inhibitor, K and Kj the dissociation constants of the complexes between enzyme and suba FIG.

W e do not know what fraction of the acetylcholine released must be hydrolyzed and within what period of time to permit the return of Na conductance to its normal level. 0 msec. On this basis one would arrive at a ratio of one molecule of acetylcholine metabolized for 500-1000 Na ions entering the fiber. The process may, of course, be slightly faster or slower, which would change the ratio correspondingly. These figures, although only approximations, appear to be of an order of magnitude quite appropriate for a trigger process accelerating the movement of Na by removing charges or opening a barrier in some other way.

These investigators found that the esterase of red blood cells differs markedly from that in the serum: the enzyme of xed blood cells has a well-defined optimum of substrate concentration. Excess of substrate decreases the activity of the enzyme. This is in sharp contrast to the activity of serum esterase which has no well-defined optimum of substrate concentration but shows the usual Michaelis-Menten type of curve of activity substrate concentration relationship. If a methyl group is attached to the carbon atom next to the ester link, as in acetyl-P-methylcholine, the compound is hydrolyzed by red cell esterase, although at a lower rate.

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