Zobrazeno 1 - 7
of 7
pro vyhledávání: '"J. N. Earnhardt"'
Autor:
J. N. Earnhardt, Philip J. Laipis, David N. Silverman, Chingkuang Tu, S. K. Wright, Ronald E. Viola, Minzhang Qian
Publikováno v:
Archives of Biochemistry and Biophysics. 361:264-270
The rate-limiting step in the catalysis of the hydration of CO2 by carbonic anhydrase involves transfer of protons between zinc-bound water and solution. This proton transfer can be enhanced by proton shuttle residues within the active-site cavity of
Publikováno v:
Journal of neurotrauma. 19(9)
Free radical-mediated mechanisms of cellular damage have been implicated in the early stages of spinal cord injury (SCI). Manganese superoxide dismutase (MnSOD) is a potent scavenger of superoxide radicals and likely serves an important cytoprotectiv
Autor:
A. V. C. Tabernilla, F. Evelyn, M. Dobrzeniecka, Douglas K. Anderson, L. William, B. McCray, J. N. Earnhardt, Harry S. Nick, B. E. Keeler
Publikováno v:
Journal of Neurochemistry. 81:106-107
A unique gene expression pattern/transcriptome characterizes the presentation of every disease state. Strategies for identification of gene families with altered expression patterns offer an information rich approach to initially assess the relevance
Publikováno v:
Journal of Neurochemistry. 81:106-107
Autor:
Nils Bergenhem, J. N. Earnhardt, David N. Silverman, Chingkuang Tu, Maha M. Lakkis, Richard E. Tashian, P. J. Laipis, Minzhang Qian
Publikováno v:
Biochemistry. 37(30)
Carbonic anhydrase VII (CA VII) appears to be the most highly conserved of the active mammalian carbonic anhydrases. We have characterized the catalytic activity and inhibition properties of a recombinant murine CA VII. CA VII has steady-state consta
Publikováno v:
Biochemistry. 37(20)
The hydration of CO2 catalyzed by carbonic anhydrase requires proton transfer from the zinc-bound water at the active site to solution for each cycle of catalysis. In the most efficient of the mammalian carbonic anhydrases, isozyme II, this transfer
We investigated the efficiency of glutamic acid 64 and aspartic acid 64 as proton donors to the zinc-bound hydroxide in a series of site-specific mutants of human carbonic anhydrase III (HCA III). Rate constants for this intramolecular proton transfe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::105238e616cb0c4c2da792ebd5fc971a
https://europepmc.org/articles/PMC1299658/
https://europepmc.org/articles/PMC1299658/