By Alton Meister
Advances in Enzymology and comparable components of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative experiences of the newest discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unequalled view of the ancient improvement of enzymology. The sequence bargains researchers the newest realizing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic strategy, and their program in either the laboratory and undefined. each one quantity within the sequence good points contributions via prime pioneers and investigators within the box from around the globe. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of themes and lengthy historic pedigree, Advances in Enzymology and comparable parts of Molecular Biology can be utilized not just through scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally via any scientist drawn to the invention of an enzyme, its homes, and its functions.
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Additional resources for Advances in Enzymology and Related Areas of Molecular Biology, Volume 21
Since about half of the cytochrome c of the liver is associated with the mitochondria and the remainder is present in the soluble fraction, one wonders whether the soluble, the particulate, or the added cytochrome c was labeled in these experiments. It should be possible to determine this by attempting to incorporate valine into the soluble cytochrome c in the presence of liver microsomes and an ATP generating system such as was used in the earlier work on amino acid incorporation, or alternatively by reisolating the mitochondria from the incubation mixture, prior to isolating the cytochrome c.
The latter is especially interesting in view of the fact that mitochondria do contain a highly active adenylate kinase which enables these granules to phosphorylate aderiylic acid (see above). All of the natural deoxynucleotides, with the exception of deoxyguanylate. have also been reported to be phosphorylated during oxidative phosphorylation by mitochondria1 preparations (326-328). Just what role the mitochondria play in this process remains to be clarified, however. Whether deoxyadenylate is a direct acceptor during oxidative phosphorylation, and also a substrate for the mitochoridrial adenylate kinase must yet be determined.
Phosphate esterification. Recent experiments of Slater and his co-workers (235-237) have provided support for this point of view. 4. The latter was the only one that displayed appreciable activity in intact mitochondria. Its activity was not increased by dinitrophenol but was increased by aging and by freezing. The activities at the other pH optima were all increased by dinitrophenol. These workers also reported that oxidative phosphorylation had optimum P:O ratios at the same pH values as the dinitrophenol-activated ATPase, and that the number of optimum P:O values with a given substrate was the same as the num-8 ber of phosphorylations coupled with the oxidation of the substrate.
Advances in Enzymology and Related Areas of Molecular Biology, Volume 21 by Alton Meister