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 expert view of the mind. Too frequently, interdisci plinary choices are at first beautiful yet end up to recite simple biochemical considera tions. now we have come to think that there at the moment are sufficiently huge numbers of neurochemists to aid a really expert enterprise comparable to the current one. we now have started with attention of conventional parts of neurochemistry which convey significant clinical job. we are hoping they'll serve the neurochemist either for common 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 jot down a bankruptcy. We plan sometimes additionally to provide reports of parts no longer thoroughly within the area of neurochemistry which we however suppose to be sufficiently well timed to be known as to the eye of all who use chemical ideas and instruments so as to higher comprehend the mind. The contributions to the current quantity pursue those ambitions. We think the sequence has set excessive criteria and has endured to uphold them. in response to the primary said 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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Additional resources for Advances in Neurochemistry
It is only with the transamination reaction that there is some ambiguity in this identification, for it is now clear that there are at least two, and perhaps three, enzymes that can catalyze the transamination of phenylalanine to phenylpyruvate. In 1964, it was reported that tyrosine aminotransferase (TAT), a cytoplasmic enzyme in liver, which is specific for aketoglutarate as the amino acceptor, can utilize phenylalanine as well as other aromatic amino acids (Jacoby ~~ LaDu, 1964). The reported results indicated that tyrosine aminotransferase could account for most of phenylalanine transamination under the assay conditions used.
Human liver data. , 1973). r value at 37'C and in the absence of lysolecithin. ,O-liberation assay (Mi1stien, Puschel, and Kaufman, unpublished results). The Km for phenylalanine for the human liver enzyme is taken from the paper by Friedman and Kaufman (1973). 08 mM phenylalanine has been corrected for the less-than-saturating content of tetrahydrobiopterin that is found in liver. 0265 /Lmol per minute per gram of tissue. • The Km for protein synthesis was estimated from data for the rat liver system at 37'C (Zamecnik and Keller, 1954).
The decrease in phenylalanine concentration as a function of time did not fall off as fast as demanded by first-order kinetics, nor did the rate of decline remain as constant as demanded by zero-order kinetics). Similar results were obtained for· more than half the controls and PKU heterozygotes that were studied by Rampini et al. (1969). Thus, the prediction based on the theoretical model for phenylalanine metabolism-that the kinetics of decline in phenylalanine blood levels should be between zero and first order-appears to have been fulfilled in the great majority of the 60 cases that were examined in these two studies.
Advances in Neurochemistry by Seymour Kaufman (auth.), B. W. Agranoff, M. H. Aprison (eds.)