Makale
Tam Makale
Uluslararası
1997
Electron spin resonance studies on cobalt carbonic anhydrase-substrate complexes
TURKISH JOURNAL OF CHEMISTRY
Cilt 21 · Sayı 2 · ss. 134–138 · 01.01.1997
Özet
The native zinc atom of bovine erythrocyte carbonic anhydrase purified by affinity choromatography was removed by dialysis against pyridine 2,6-dicarboxylic acid. Cobalt carbonic anhydrase was prepared from the zinc-free apoenzyme. The binding conditions of CO2 and p-nitrophenylacetate to cobalt carbonic anhydrase were investigated by electron spin resonance at different pH levels.
Anahtar kelimeler
ZINC
SITE
BINDING
MECHANISM
bovine carbonic anhydrase
ESR spectroscopy
substrate complexes
Atıf için künye
NUHOGLU, C., Demir, N., NALBANTOGLU, B., Küfrevioğlu, Ö. İ., YOGURTCU, Y., Özdemir, H., & AYYILDIZ, E. (1997). Electron spin resonance studies on cobalt carbonic anhydrase-substrate complexes. TURKISH JOURNAL OF CHEMISTRY, 21(2), 134–138.
BibTeX
@article{nuhoglu1997-67336,
author = {NUHOGLU, C and Demir, Nuray and NALBANTOGLU, B and Küfrevioğlu, Ömer İrfan and YOGURTCU, YK and Özdemir, Hasan and AYYILDIZ, Eyüp},
title = {Electron spin resonance studies on cobalt carbonic anhydrase-substrate complexes},
journal = {TURKISH JOURNAL OF CHEMISTRY},
year = {1997},
volume = {21},
number = {2},
pages = {134--138},
issn = {1010-7614},
url = {https://akademik.atauni.edu.tr/yayinlar/67336-electron-spin-resonance-studies-on-cobalt-carbonic-anhydrase-substrate-complexes}
}