Membrane-Bound Enzymes: Proceedings of an International by R. M. C. Dawson, P. J. Quinn (auth.), Giuseppe Porcellati,

By R. M. C. Dawson, P. J. Quinn (auth.), Giuseppe Porcellati, Fernando di Jeso (eds.)

The current quantity includes the entire papers provided on the overseas convention on Membrane-Bound Enzymes held at Pavia in may perhaps 1910. The book of its clinical content material has been made attainable through the collaboration of many scientists who've taken half on the Symposium and who deeply and actively mentioned the lectures which have been introduced. with the intention to ascertain speedy pu­ blication, despite the fact that, the dialogue aren't pronounced right here. the final topic of membrane-bound enzymic task, its habit, localization and rules, was once explored extensive from the standpoints of a number of the individuals in biophysics, bioche­ mistry, cytology and pharmacology. every one consultation was once in brief in­ troduced by way of the consultation chairman's comments concerning the box lower than dialogue. on the finish of the convention, Dr.R.M.C.Dawson made a few concluding comments. The assembly is taken into account to were very winning. It definitely gave one other stimulus to biochemical and physiological study staff during this box of analysis. The editors show their due to the authors of the papers and to the Plenum Publishing company for the urged reaction which has enabled the swift ebook of the amount, and to the auditorium of the assembly, which used to be attended via a couple of hundred examine staff con­ cerned with the issues of membrane biology. we're satisfied to recognize the monetary help of assorted firms, which were indexed in one other a part of this book.

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1 and ref. 8). 44 QUAGLIARIELLO, PAPA, LOFRUMENTO, MEIJER, AND TAGER TABLE III Exchange of Intramitochondrial «-Oxoglutarate with Extramitochondrial Malonate. 5), 3 mM MgC12' 1 mM arsenite, 20 mM glucose and hexokinase. 5 mM ~4C] Malonate and 10 mM butylmalonateo After 2 min mitochondria were centrifuged from the suspending medium (see ref. 29). 1 85 93 0 56 -25 -23 +18 +29 Pi-loaded mitochondria took up twice as much (14c] malate as unloaded mitochondria. In the unloaded mitochondria the residual amounts of endogenous ~ioniC substrates must have been responsible for the uptake of(1 c] malate.

From ref. 42). Additions None DNP t 100 pM Mersalyl 110 pM Mersalyl+Cysteine 1 mM 32p. in the ~atrix (nmoles) 255 108 16 251 Pi-induced cytochrome c reduction, absorbance increase at 550 vs 540 II9l Log. 10/1 18 x 10-3 o o 18 x 10-3 ANION TRANSLOCATION SYSTEMS" 53 cytochrome c. The response of respirator,y chain to Pi appears to be correlated with the uptake of Pi by mitochondria. The experiment of Table VIII shows that Pi, added in the presence of oligomycin, to Pi-depleted mitochondria, was actively accumulated by mitochondria.

Most critical is the question of the mechanism of proton translocation. Mitchell has been the first to recognize that the basic problem of the mitochondrial ion translocation process is that concerning the protons (8). In fact on one hand the lipid layer behave as proton impermeable (9) and on the other the energized mitochondria are able to extrude and take up proton at a very high rate (3). The contention of Mitchell has been disputed until very recently by Chance (10-11) \\7ho has maintained for a long time that the mitochondrial membrane is highly permeable to protons and therefore no special mechanism for proton translocation is needed.

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