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 before everything beautiful yet prove to recite easy biochemical considera tions. we've come to think that there are actually sufficiently huge numbers of neurochemists to help a really expert enterprise resembling the current one. we've all started with attention of conventional parts of neurochemistry which express significant clinical task. we are hoping they'll serve the neurochemist either for normal interpreting and for specialised details. The reader also will be able to mirror at the unbridled hypothesis that effects from the disinhibiting results at the writer who has been invited to put in writing a bankruptcy. We plan sometimes additionally to provide reports of parts now not thoroughly within the area of neurochemistry which we however suppose to be sufficiently well timed to be referred to as to the eye of all who use chemical ideas and instruments in order to larger 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. based on the main acknowledged within the final paragraph of the Preface quantity 1, we contain during this quantity Koshland's "Sensory reaction in micro organism" (Chapter 5).
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1966). In the basal state, therefore, phenylalanine in muscle cells is not equilibrated with the phenylalanine in the plasma water. 2. Despite the higher concentration of phenylalanine in muscle than in plasma, the muscle can sustain stiD higher concentrations of phenylalanine (relative to phenylalanine in BIOCHEMICAL MECHANISMS OF PHENYLKETONURIA 39 the sum of the phenylalanine hydroxylase plus the transaminase velocities shown in Figure 6 is probably not in great error. Since we have already reached the same conclusion about the transaminase velocities, we can conclude that the phenylalanine hydroxylase data are also reasonably accurate.
Other enzymes may be present that can degrade the substrate, an essential cofactor, or the product, and inhibitors or activators BIOCHEMICAL MECHANISMS OF PHENYLKETONURIA 25 may influence the reproducibility of results. These difficulties are compounded when the enzyme being studied is part of a complex system, as is the case with phenylalanine hydroxylase. In addition, as will be discussed, it is now clear that PKU is not a single entity, but rather is a heterogeneous group of diseases. In the face of this complexity, of both biochemical and genetic origin, the field has been ill-served by the gratuitous element of chaos that is introduced with the use of in vitro assays for phenylalanine hydroxylase, which may not be reliable.
The potential hazards in the assay of phenylalanine hydroxylase that have just been discussed have been encountered, ironically, because phenylalanine hydroxylase activity is deceptively easy to measure in normal human and some animal liver extracts. The error introduced by, for example, reliance on measurements of tyrosine formation (determined either ftuorometrically or colorimetrically), rather than on measurements ofradioactive tyrosine formed from radioactive phenylalanine, is insignificant when phenylalanine hydroxylase activity is determined in normal liver.