摘要
从乳酸杆菌发酵液经过两次柱层析，可以得到纯度较高的乳酸脱氢酶，酶的比活力高达６７８．９ｕ／ｍｇ，纯度提高８５．７倍。酶的热稳定性好，ｐＨ稳定范围较宽，在临床上可用于雨氨酸氨基较移酶活力的测定。
Lactate dehydrogenase from Lactobacillus SP.L15 was purified with DEAE-cellulosechromatography and hydroxyapatitate chromatography. Its specific activity increased by 85.7-fold to 678.9u/mg protein. Its thermal stability. pH stability.optiumum PH and Kmvalue were determined. It can be used determining activily of alanine aminotransferase inclinic.
出处
《生物技术》
CAS
CSCD
1999年第1期11-15,共5页
Biotechnology
