| 细菌乳酸脱氢酶的纯化及其性质研究 |
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| 引用本文： | 郑国爱. 细菌乳酸脱氢酶的纯化及其性质研究[J]. 生物技术, 1999, 9(1): 11-15 |
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| 作者姓名： | 郑国爱 |
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| 作者单位： | 广东燕塘生物化学药业有限公司,广州,510507 |
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| 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。
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| 关 键 词： | 乳酸脱氢酶 纯化 |
| 修稿时间： | 1998-06-05 |
STUDIES ON PURIFICATION AND PROPERTIES OF LACTOBACILLUS LACTATE DEHYDROGENASE |
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| Zhen Guoai. STUDIES ON PURIFICATION AND PROPERTIES OF LACTOBACILLUS LACTATE DEHYDROGENASE[J]. Biotechnology, 1999, 9(1): 11-15 |
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| Authors: | Zhen Guoai |
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| Affiliation: | Guangdong Yantang Biochemistry Pharmaceutical Co.Ltd.Guangzhou;;510507 |
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| Abstract: | 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. |
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| Keywords: | lactate dehydrogenase purification |
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