TY - JOUR
T1 - Cytochrome c
T2 - A Thermodynamic Study of Relationships among Oxidation State, Ion‐Binding and Structural Parameters: 2. Ion‐Binding Linked to Oxidation State
AU - Margalit, Rimona
AU - SCHEJTER, Abel
PY - 1973/2
Y1 - 1973/2
N2 - The specific binding of anions to oxidized horse‐heart cytochrome c has been studied by two methods: measuring the effect of ion concentration on the redox potential, and directly by gel nitration. The anions investigated were: chloride, phosphate, ADP and sulfanilate. The binding constants estimated are in the range of 1–10 mM−1, and the number of sites per protein molecule are 1 to 2. The specificity of anion binding to the oxidized protein is demonstrated.
AB - The specific binding of anions to oxidized horse‐heart cytochrome c has been studied by two methods: measuring the effect of ion concentration on the redox potential, and directly by gel nitration. The anions investigated were: chloride, phosphate, ADP and sulfanilate. The binding constants estimated are in the range of 1–10 mM−1, and the number of sites per protein molecule are 1 to 2. The specificity of anion binding to the oxidized protein is demonstrated.
UR - http://www.scopus.com/inward/record.url?scp=0015576060&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1973.tb02634.x
DO - 10.1111/j.1432-1033.1973.tb02634.x
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AN - SCOPUS:0015576060
SN - 0014-2956
VL - 32
SP - 500
EP - 505
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 3
ER -