Download PDF by Seymour Kaufman (auth.), B. W. Agranoff, M. H. Aprison: Advances in Neurochemistry

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By Seymour Kaufman (auth.), B. W. Agranoff, M. H. Aprison (eds.)

In the Preface to quantity 1, we acknowledged: This sequence acknowledges that investigators who've entered neurochemistry from the biochemical culture have a slightly really good view of the mind. Too frequently, interdisci­ plinary choices are before everything appealing yet prove to recite simple biochemical considera­ tions. we've come to think that there are actually sufficiently huge numbers of neurochemists to help a really expert enterprise akin to the current one. now we have began with attention of conventional components of neurochemistry which exhibit huge clinical job. we are hoping they're going to serve the neurochemist either for normal examining and for specialised info. The reader also will have the ability to mirror at the unbridled hypothesis that effects from the disinhibiting results at the writer who has been invited to write down a bankruptcy. We plan sometimes additionally to provide stories of components now not thoroughly within the area of neurochemistry which we however believe to be sufficiently well timed to be referred to as to the eye of all who use chemical ideas and instruments which will greater comprehend the mind. The contributions to the current quantity pursue those objectives. We think the sequence has set excessive criteria and has persevered to uphold them. in keeping with the primary acknowledged within the final paragraph of the Preface quantity 1, we comprise during this quantity Koshland's "Sensory reaction in micro organism" (Chapter 5).

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That this assumption is reasonable is indicated by the reported Km value of 13 mM for phenylalanine for rat liver phenylalanine-pyruvate transaminase at 25°C (Lin et al.. 1958). d The values for the cytoplasmic enzyme are for the noninduced rat liver tyrosine aminotransferase and were determined at 37'C (Jacoby and LaDu, Km (mM) Vrna,. 08 mM phenylalanine (jLmoUrnin per g) TABLE 3. ~ V, Vo §a ~ s: ~ ~ <: ~ ~ ~ ~ CI) 2;; ~ g ~ Q t-< ~ ..... g a 36 CHAPTER 1 that the values cover a 600-fold range of phenylalanine concentration, with the Km for protein synthesis being the lowest, followed by the Km for the hydroxylase, and the transaminase having the highest value.

Using the assumption stated-that phenylalanine in plasma and interstitial water does not equilibrate rapidly with phenylalanine in intracellular water-the theoretical rate of decline of plasma phenylalanine concentration was calculated from the sum of the rates of phenylalanine hydroxylase and the transaminase shown in Figure 6. The calculations were made for successive 30-min periods, starting with the zero time plasma phenylalanine concentration of about 10 mgtl00 m1 that was reported for normal adults after an intravenous dose of 50 mg phenylalanine per kilogram of body weight (Bremer and Neumann, 1966b).

It is not known, however, whether the properties of the soluble and mitochondrial enzymes are the same. , 1972), there are reasons for believing that the cytoplasmic phenylalanine-pyruvate transaminase does not playa major role in phenyla1anine transamination in the whole organism. , 1972) that also utilizes pyruvate as a substrate, alanine-glutamate transaminase. 9 mM (Hopper and Segal, 1962). Both the lower activity and the poorer Km for pyruvate would indicate that little of the potential activity of phenylalanine-pyruvate transaminase would be expressed in the presence of an active alanine-glutamate transaminase.

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