D-Lactate dehydrogenase (cytochrome) was isolated from baker´s yeasts (Saccharomyces cerevisiae) using fast protein liquid chromatography. Mitochondria from disrupted cells were separated and enzymes released by Triton X-100. Purification was performed by fast protein liquid chromatography on hydroxylapatite and in another separate experiment on AH-Sepharose with covalently bound 4-hydroxy-acyanocinnamic acid (SHCA). Although purification on hydroxylapatite provided approachable samples with activities for only D-lactic acid, chromatography on SHCA seemed to be better because a purified fraction of enzyme with the specific activity of 3.38 nkat/mg was obtained. Another problem considered was the usefulness of the combination of chromatography on hydroxylapatite and SHCA providing a fraction of D-lactic acid with specific activity of 5.71 nkat/mg and no cross reactivity for L-lactic acid.
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.