Kinetic and thermodynamic studies on the disulfide-bond reducing potential of hydrogen sulfide.
Nitric Oxide. 2015.
PMID: 25512332
Search Page
Filters
Results by year
Table representation of search results timeline featuring number of search results per year.
| Year | Number of Results |
|---|---|
| 1989 | 1 |
| 1992 | 1 |
| 2014 | 1 |
| 2015 | 1 |
| 2025 | 0 |
Search Results
3 results
Results by year
Citations
1
article
found by citation matching
Search results
Page 1
Did you mean
kinetic and thermodynamic studies on the disulfide bond inducing potential of hydrogen sulfide.
(1 results)?
Kinetic and thermodynamic studies on the disulfide-bond reducing potential of hydrogen sulfide.
Nitric Oxide. 2015 Apr 30;46:93-101. doi: 10.1016/j.niox.2014.12.003. Epub 2014 Dec 12.
Nitric Oxide. 2015.
PMID: 25512332
The significance of persulfide species in hydrogen sulfide biology is increasingly recognized. However, the molecular mechanisms of their formation remain largely elusive. The obvious pathway of the reduction of biologically abundant disulfide moieties by sulfide …
The significance of persulfide species in hydrogen sulfide biology is increasingly recognized. However, the molecular mechanis …
Contribution of the 6-120 disulfide bond of alpha-lactalbumin to the stabilities of its native and molten globule states.
Biochemistry. 1992 Dec 22;31(50):12695-700. doi: 10.1021/bi00165a021.
Biochemistry. 1992.
PMID: 1472507
The unfolding and refolding of a derivative of alpha-lactalbumin, in which the disulfide bond between Cys6 and Cys120 is selectively reduced and S-carboxymethylated, are investigated by equilibrium and kinetic circular dichroism measurements. ...The st …
The unfolding and refolding of a derivative of alpha-lactalbumin, in which the disulfide bond between Cys6 and Cys120 is selec …
Extrinsic 33-kilodalton protein of spinach oxygen-evolving complexes: kinetic studies of folding and disulfide reduction.
Biochemistry. 1989 Sep 5;28(18):7188-93. doi: 10.1021/bi00444a009.
Biochemistry. 1989.
PMID: 2684273
The disulfide bond was reduced even in the absence of guanidine hydrochloride. The unfolding and refolding kinetics of the 33-kDa protein using guanidine hydrochloride were also studied under the same conditions, and the results were compared with thos …
The disulfide bond was reduced even in the absence of guanidine hydrochloride. The unfolding and refolding kinetics …
Cite