Covalent Binding and Interstrand Cross-Linking of Duplex DNA by Dirhodium(II,II) Carboxylate Compounds†

Biochemistry ◽  
2005 ◽  
Vol 44 (3) ◽  
pp. 996-1003 ◽  
Author(s):  
Shari U. Dunham ◽  
Helen T. Chifotides ◽  
Szymon Mikulski ◽  
Amity E. Burr ◽  
Kim R. Dunbar
1996 ◽  
Vol 317 (2) ◽  
pp. 509-514 ◽  
Author(s):  
James M. SALHANY ◽  
Renee L. SLOAN ◽  
Lawrence M. SCHOPFER

Band 3 Memphis variant II is a mutant anion-exchange protein associated with the Diego a+ blood group antigen. There are two mutations in this transporter: Lys-56 → Glu within the cytoplasmic domain, and Pro-854 → Leu within the membrane-bound domain. The Pro-854 mutation, which is thought to give rise to the antigenicity, is located within the C-terminal subdomain of the membrane-bound domain. Yet, there is an apparent enhancement in the rate of covalent binding of H2DIDS (4,4´-di-isothiocyanatodihydro-2,2´-stilbenedisulphonate) to ‘lysine A’ (Lys-539) in the N-terminal subdomain, suggesting widespread conformational changes. In this report, we have used various kinetic assays which differentiate between conformational changes in the two subdomains, to characterize the stilbenedisulphonate site on band 3 Memphis variant II. We have found a significantly higher H2DIDS (a C-terminal-sensitive inhibitor) affinity for band 3 Memphis variant II, due to a lower H2DIDS ‘off’ rate constant, but no difference was found between mutant and control when DBDS (4,4´-dibenzamido-2,2´-stilbenedisulphonate) (a C-terminal-insensitive inhibitor) ‘off’ rates were measured. Furthermore, there were no differences in the rates of covalent binding to lysine A, for either DIDS (4,4´-di-isothiocyanato-2,2´-stilbenedisulphonate) or H2DIDS. However, the rate of covalent intrasubunit cross-linking of Lys-539 and Lys-851 by H2DIDS was abnormally low for band 3 Memphis variant II. These results suggest that the Pro-854 → Leu mutation causes a localized conformational change in the C-terminal subdomain of band 3.


Author(s):  
Ahmed Mostafa Abdelhady ◽  
Kazumitsu Onizuka ◽  
Kei Ishida ◽  
Sayaka Yajima ◽  
Eriko Mano ◽  
...  

2012 ◽  
Vol 44 ◽  
pp. 94-95
Author(s):  
Y. Satyawali ◽  
P. Jochems ◽  
S. Van Roy ◽  
W. Doyen ◽  
W. Dejonghe ◽  
...  

1991 ◽  
Vol 113 (20) ◽  
pp. 7765-7766 ◽  
Author(s):  
Jeng Pyng Shaw ◽  
John Milligan ◽  
Steven H. Krawczyk ◽  
Mark Matteucci

2010 ◽  
Vol 122 (34) ◽  
pp. 6093-6096 ◽  
Author(s):  
Huan Wang ◽  
Steven E. Rokita

Molecules ◽  
2018 ◽  
Vol 23 (4) ◽  
pp. 828 ◽  
Author(s):  
Siddhant Sethi ◽  
Shigetaka Nakamura ◽  
Kenzo Fujimoto
Keyword(s):  

2005 ◽  
Vol 17 (02) ◽  
pp. 101-107 ◽  
Author(s):  
PEI-RU CHEN ◽  
PEI-LEUN KANG ◽  
WEN-YU SU ◽  
FENG-HUEI LIN ◽  
MING-HONG CHEN

The thermal and degradable properties of carbodiimide (EDC) or glutaraldehyde (GTA) cross-linked gelatin membranes have been investigated in order to evaluate the effects of different concentrations of two kinds of cross-linking reagent on the stability of membranes. In the thermogram recorded from a gelatin membrane cross-linked with EDC solution, the endothermic peak of 0.8% EDC cross-linking gelatin was centered at about 61°C that was higher than other samples treated with EDC solutions. Denaturation temperature (Td) of gelatin samples increased on increasing EDC concentration (0.2% to 0.8%), in agreement with the simultaneous increased of the extent of cross-linking. But increasing GTA concentration from 0.05% to 0.6%, the Td values of gelatin samples were decreased from 66.2°C to 56.3°C . In addition, two endothermic peaks were observed in 0.4% and 0.6% GTA cross-linking groups because of the GTA concentration was too high to complete cross-linking reaction. Therefore, partial of gelatin membrane was cross-linked completely but others were not. In the thermogravimetric analysis, the proportion of cracking endothermic peak of 0.6% GTA cross-linking gelatin (g15G0.6) was higher than the peak of 0.6% EDC cross-linking gelatin (g15C0.6). Therefore, g15G0.6 cracked to smaller molecules has to absorb more calorific capacity than g15C0.6. The increase in the strength of covalent binding on increasing the proportion of endothermic peak was evident. The results of degradable rate were in agreement with the lower concentration of cross-linked reagent the faster degraded rate of gelatin membrane. The MTT assay showed that 15% gelatin cross-linked by 0.8% EDC has the least cytotoxicity, and cell activity of this group was similar to control group (blank dish). As the concentration of GTA in gelatin membranes was down to 0.05% or 0.1% the cell viability was returned to approach the value of control group.


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