scholarly journals Kinetic Studies by Means of the NMR Techniques. I. Acid-Catalyzed Proton-Exchange Reactions of Some Substituted Phenols

1988 ◽  
Vol 61 (10) ◽  
pp. 3393-3397 ◽  
Author(s):  
Akihiro Yoshino ◽  
Yasuki Nakashima ◽  
Kensuke Takahashi
Keyword(s):  
Kinetic Studies ◽  
Proton Exchange ◽  
Exchange Reactions ◽  
Substituted Phenols ◽  
Nmr Techniques ◽  
Acid Catalyzed

Proton exchange reactions of C2–C4 alkanes sorbed in ZSM-5 zeolite

2012 ◽  
Vol 131 (6) ◽  
Author(s):  
Kanjarat Sukrat ◽  
Daniel Tunega ◽  
Adelia J. A. Aquino ◽  
Hans Lischka ◽  
Vudhichai Parasuk
Keyword(s):  
Proton Exchange ◽  
Exchange Reactions

Hydrocarbon-Carbanion Proton Exchange Reactions in Dimethyl Sulfoxide

1967 ◽  
Vol 89 (7) ◽  
pp. 1728-1730 ◽  
Author(s):  
John I. Brauman ◽  
Donald F. McMillen ◽  
Yoko. Kanazawa
Keyword(s):  
Dimethyl Sulfoxide ◽  
Proton Exchange ◽  
Exchange Reactions

KINETIC STUDIES ON THE ACID-CATALYZED PUMMERER REACTION OF α-(METHYLSULFINY)ACETOPHENONES

1983 ◽  
Vol 16 (1-2) ◽  
pp. 223-232 ◽  
Author(s):  
Norio Kunieda ◽  
Yoichi Fujiwara ◽  
Akira Suzuki ◽  
Masayoshi Kinoshita
Keyword(s):  
Kinetic Studies ◽  
Pummerer Reaction ◽  
Acid Catalyzed

scholarly journals Hydrogen production and deuterium-proton exchange reactions catalyzed by Desulfovibrio nickel(II)-substituted rubredoxins

1988 ◽  
Vol 85 (24) ◽  
pp. 9378-9380 ◽  
Author(s):  
P. Saint-Martin ◽  
P. A. Lespinat ◽  
G. Fauque ◽  
Y. Berlier ◽  
J. LeGall ◽  
...  
Keyword(s):  
Hydrogen Production ◽  
Proton Exchange ◽  
Exchange Reactions

Kinetic Studies of Copper(II)-exchange from L-Histidine to Human Serum Albumin and Diglycyl-L-histidine, a Peptide Mimicking the Copper(II)-transport Site of Albumin

1975 ◽  
Vol 53 (5) ◽  
pp. 710-715 ◽  
Author(s):  
Show-Jy Lau ◽  
Bibudhendra Sarkar
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Exchange Rates ◽  
Human Serum ◽  
Kinetic Studies ◽  
Side Chain ◽  
Exchange Reactions ◽  
Equilibrium Study ◽  
Rate Determining Step ◽  
The Difference

The Cu(II)-exchange reactions of L-histidine with human serum albumin and diglycyl-L-histidine were studied at pH 7.53 in 0.1 MN-ethylmorpholine–HCl buffer. The exchange rates from L-histidine to albumin and peptide were determined as 0.67 and 0.42 s−1 respectively. Those from albumin and peptide to L-histidine were obtained as 0.04 and 0.07 s−1 respectively. This result is in accord with the earlier observations of the equilibrium study that the peptide has about half the Cu(II)-binding affinity as compared to albumin. The difference in the Cu(II)-exchange rates of albumin and peptide may reflect the influence of either the COOH-terminal free carboxyl group of the peptide or the side-chain residues of the Cu(II)-binding site in the native protein or both. An exchange mechanism is proposed in which the ternary complexes are shown to play the important role in the rate-determining step in the Cu(II)-exchange between a macromolecule and a small substance.

scholarly journals A mitochondrial monocarboxylate transporter in rat liver and heart and its possible function in cell control

1975 ◽  
Vol 148 (1) ◽  
pp. 41-47 ◽  
Author(s):  
J Mowbray
Keyword(s):  
Pyruvate Dehydrogenase ◽  
Mitochondrial Membrane ◽  
Pyruvate Dehydrogenase Complex ◽  
Animal Experiments ◽  
Kinetic Studies ◽  
Monocarboxylate Transporter ◽  
Keto Acid ◽  
Exchange Reactions ◽  
Transport Inhibitors

Several hydroxy- and keto-substituted monocarboxylates were found to undergo co- as well as counter-exchange across the mitochondrial membrane. The results argue against a simple Donnan system and may be explained by the existence of a transporter for monocarboxylates. In support of this explanation it was apparently possible to ‘pump’ pyruvate to the sucrose-inaccessible space by using the dicarboxylate transporter. Further, several aromatic and aliphatic analogues of pyruvate, but not of di- or tri-carboxylate transport inhibitors, have been shown to prevent pyruvate-exchange reactions. Palmitoylcarnitine was found to have a much stronger affinity for the carrier than either carnitine or pyruvate and the possible consequences of this for carnitine-palmitoylcarnitine exchange and on the control of the pyruvate dehydrogenase complex are explored. In view of the range of transport inhibitors and substrates it is suggested that the carrier has a fairly broad specificity. ‘Inhibitor-stop’ kinetic studies show that the speed of translocation of pyruvate at 1 degrees C is of the same order as malate. The possible correlation between the role of a hydroxy-keto acid transporter in substrate exchange and some whole animal experiments is briefly discussed. It is proposed that for reasons of control the cell will require membrane monocarboxylate transporters no less than di- or tri-carboxylate carriers.

Sign in / Sign up

Export Citation Format

Share Document