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用ＤＥＡＥ－ｓｅｐｈａｃｅｌ和ＣＭ－ｃｅｌｕｌｏｓｅ柱层析的方法从Ｃｏｍａｍｏｎａｓｔｅｓｔｏｓｔｅｒｏｎｉ菌体中纯化得到一定纯度的脱辅基的乙醇脱氢酶。在含３ｍＭＣａＣｌ２的Ｔｒｉｓ／ＨＣｌ缓冲液（２０ｍＭ，ｐＨ７．０）中，该酶能与ＰＱＱ重组成有活性的全酶，测出的全酶活性大小与外加ＰＱＱ的量成正比，从而定量分析ＰＱＱ。该法专一、灵敏、可靠。
Purification of CoAmonastestosteroni cells with DEAE-sephacel and CM-celulose afforded a pure apo-alcohol dehydrogenase. In Tris-HCl buffer (20 mM, pH 7.0) containing 3 mM CaCl 2, the enzyme is capable of recombining with PQQ to become an active holoenzyme. The measured total enzyme activity is proportional to the amount of added PQQ to quantitatively analyze PQQ . The law is specific, sensitive and reliable.