通过亲和色谱法评估乳酸脱氢酶同工酶与还原型烟酰胺腺嘌呤二核苷酸相互作用的平衡常数。
Evaluation of equilibrium constants for the interaction of lactate dehydrogenase isoenzymes with reduced nicotinamide-adenine dinucleotide by affinity chromatography.
作者信息
Brinkworth R I, Masters C J, Winzor D J
出版信息
Biochem J. 1975 Dec;151(3):631-6. doi: 10.1042/bj1510631.
Abstract
Rabbit muscle lactate dehydrogenase was subjected to frontal affinity chromatography on Sepharose-oxamate in the presence of various concentrations of NADH and sodium phosphate buffer (0.05 M, pH 6.8) containing 0.5 M-NaCl. Quantitative interpretation of the results yields an intrinsic association constant of 9.0 x 10 (4)M-1 for the interaction of enzyme with NADH at 5 degrees C, a value that is confirmed by equilibrium-binding measurements. In a second series of experiments, zonal affinity chromatography of a mouse tissue extract under the same conditions was used to evaluate assoication constants of the order 2 x 10(5)M-1, 3 x 10(5)M-1, 4 x 10(5)M-1, 7 x 10(5)M-1 and 2 x 10(6)M-1 for the interaction of NADH with the M4, M3H, M2H2, MH3 and H4 isoenzymes respectively of lactate dehydrogenase.
摘要
在含有0.5M氯化钠的不同浓度的NADH和0.05M磷酸钠缓冲液（pH6.8）存在的条件下，将兔肌肉乳酸脱氢酶进行Sepharose-草氨酸盐前沿亲和层析。对结果的定量解释得出，在5℃时酶与NADH相互作用的固有缔合常数为9.0×10⁴M⁻¹，该值通过平衡结合测量得到证实。在第二系列实验中，在相同条件下对小鼠组织提取物进行区带亲和层析，以评估NADH与乳酸脱氢酶的M4、M3H、M2H2、MH3和H4同工酶相互作用的缔合常数，分别为2×10⁵M⁻¹、3×10⁵M⁻¹、4×10⁵M⁻¹、7×10⁵M⁻¹和2×10⁶M⁻¹。
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