与纯化的核酮糖二磷酸羧化酶相关的内肽酶活性的来源。

Plant Growth Laboratory and the Department of Agronomy and Range Science, University of California, Davis, California 95616.

Plant Physiol. 1984 May;75(1):74-7. doi: 10.1104/pp.75.1.74.

The association of endoproteolytic activity with purified ribulose bisphosphate carboxylase (RuBPCase) from barley (Hordeum vulgare var Numar) leaves was investigated. RuBPCase purified by chromatography on agarose gel and diethylaminoethyl-cellulose was free of associated endoproteolytic activity. The addition of leupeptin and casein to the extraction buffer completely eliminated proteolysis during initial extraction of RuBPCase. Endoproteolytic activity previously found associated with RuBPCase was identified as being due to contamination of endoproteinases from broken vacuoles.

研究了与纯化的大麦（Hordeum vulgare var Numar）叶片中的核酮糖二磷酸羧化酶（RuBPCase）相关的内切蛋白酶活性。通过琼脂糖凝胶和二乙基氨基乙基纤维素层析纯化的 RuBPCase 无相关的内切蛋白酶活性。在最初提取 RuBPCase 时，向提取缓冲液中添加亮抑酶肽和酪蛋白可完全消除蛋白水解。先前与 RuBPCase 相关的内切蛋白酶活性被鉴定为来自破裂液泡的内肽酶的污染。