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Full-Text Articles in Life Sciences
The Nature Of The "Contractile" Protein Isolated From Brain / S. Puszkin, E. Puszkin, D. D. Clarke, And S. Berl. Coll Of Phys. And Surgeons., Columbia Univ., N.Y. 10032, S. Puszkin, E. Puszkin, Donald Dudley Clarke Phd, Soll Berl
The Nature Of The "Contractile" Protein Isolated From Brain / S. Puszkin, E. Puszkin, D. D. Clarke, And S. Berl. Coll Of Phys. And Surgeons., Columbia Univ., N.Y. 10032, S. Puszkin, E. Puszkin, Donald Dudley Clarke Phd, Soll Berl
Chemistry Faculty Publications
We have described the isolation from brain of a Mg++/Ca++-ATPase resembling muscle actomyosin (Sci. 12 1 1701 1968). Like myofibrils (Perry and Grey 1 Biochem. J. 64, 184, 1956), the ATPase activity isolated from rat and cat brain is dependent upon the cone. of ATP and cation. When the conc. of ATP exceeds that of Mg++ 1 enzyme activity is inhibited. With increasing conc. of Mg++ 1 the optimum conc. of ATP also increases. This does not occur with Ca++ . Polyethylenesulfonate( PS)(I0-6M)causes the splitting of actomyosin into actin and myosin; the Mg++-ATPose activity is correspondingly diminished (Barony and Joisle …
The Dissociative Breakdown Of Negative Ions / By D. D. Clarke, Chemistry Department, Fordham University, New York, 10458, U.S.A. C. A. Coulson, Mathematical Institute, University Of Oxford, Donald Dudley Clarke Phd, C. A. Coulson
The Dissociative Breakdown Of Negative Ions / By D. D. Clarke, Chemistry Department, Fordham University, New York, 10458, U.S.A. C. A. Coulson, Mathematical Institute, University Of Oxford, Donald Dudley Clarke Phd, C. A. Coulson
Chemistry Faculty Publications
A discussion is given of the process whereby a substituted aromatic molecule captures a slow electron and dissociates. It is shown that the process often goes via two stages. and that the relative symmetries of the electroncapture state and the final dissociation state are very important. Both the sensitivity of the process to changes in the substituent and the existence of an activation energy are explained in the model
Decarboxylation Studies Of Glutamate, Glutamine, And Aspartate From Brain Labelled With [I-14]Acetate, L-[U-14c]-Aspartate, And L-[U-14c]Glutamate / W.J. Nickls And D. D. Clarke Chemistry Department, Fordham University, Bronx, N.Y. And S. Berl Department Of Neurology, College Of Physicians And Surgeons, Columbia University, New York, N.Y., William J. Nicklas, Donald Dudley Clarke Phd, Soll Berl
Decarboxylation Studies Of Glutamate, Glutamine, And Aspartate From Brain Labelled With [I-14]Acetate, L-[U-14c]-Aspartate, And L-[U-14c]Glutamate / W.J. Nickls And D. D. Clarke Chemistry Department, Fordham University, Bronx, N.Y. And S. Berl Department Of Neurology, College Of Physicians And Surgeons, Columbia University, New York, N.Y., William J. Nicklas, Donald Dudley Clarke Phd, Soll Berl
Chemistry Faculty Publications
Studies in vivo and in vitro of the distribution of label in C-1 of glutamate and glutamine and C-4 of aspartate in the free amino acids of brain were carried out. [1-14C]Acetate was used both in vivo and in vitro and L-[U-14C]aspartate and L-[U-14C]glutamate were used in vitro. (1) The results obtained with labelled acetate and aspartate suggest that CO2 and a 3-carbon acid may exchange at different rates on a CO2-fixing enzyme. (2) The apparent cycling times of both glutamate and glutamine show fast components measured in minutes and slow components measured in hours. (3) With [l-14C]acetate in vitro …