Kolk A H, van Kuyk L, Boettcher B
Biochem J. 1978 Sep 1;173(3):767-71. doi: 10.1042/bj1730767.
Human isoenzyme LDH-X (lactate dehydrogenase isoenzyme X) was isolated from seminal fluid of frozen semen samples by affinity chromatography by using oxamate-Sepharose and AMP-Sepharose. In the presence of 1.6 mM-NAD+, isoenzyme LDH-X does not bind to AMP-Sepharose, whereas the other lactate dehydrogenase isoenzymes do. This is the crucial point in the isolation of isoenzyme LDH-X from the other isoenzymes. The purified human isoenzyme LDH-X had a specific activity of 146 units/mg of protein.
通过使用草氨酸盐-琼脂糖凝胶和腺苷酸-琼脂糖凝胶亲和层析法，从冷冻精液样本的精液中分离出人类同工酶LDH-X（乳酸脱氢酶同工酶X）。在存在1.6 mM-NAD+的情况下，同工酶LDH-X不与腺苷酸-琼脂糖凝胶结合，而其他乳酸脱氢酶同工酶则会结合。这是从其他同工酶中分离同工酶LDH-X的关键点。纯化后的人类同工酶LDH-X的比活性为146单位/毫克蛋白质。
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