豌豆叶绿体的一种纯化锌蛋白酶EP1可降解核酮糖-1,5-二磷酸羧化酶/加氧酶的大亚基。
A Purified Zinc Protease of Pea Chloroplasts, EP1, Degrades the Large Subunit of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase.
作者信息
Bushnell T. P., Bushnell D., Jagendorf A. T.
机构信息
Plant Biology Section, Cornell University, Ithaca, New York 14853.
出版信息
Plant Physiol. 1993 Oct;103(2):585-591. doi: 10.1104/pp.103.2.585.
Abstract
A previously reported endopeptidase (EP1) from pea chloroplasts was purified over 11,000-fold using a four-step protocol involving ultrafiltration, sucrose gradient centrifugation, isoelectric focusing, and high performance liquid chromatography gel filtration. The enzyme was determined to be a metalloprotease requiring bound Zn2+ and added Mg2+ or Ca2+ for proper activity. Its localization in the stroma of pea chloroplasts was confirmed by demonstrating its insensitivity to thermolysin when the envelope was intact. A contaminating serine protease that attacks EP1 was found. The contaminating protease was inhibited by 4-(2-aminoethyl)-benzenesulfonyl fluoride, but not by o-phenanthroline, whereas EP1 sensitivities were the reverse. EP1 is able to hydrolyze the large subunit of native ribulose-1,5-bisphosphate carboxylase/oxygenase under physiological conditions.
摘要
先前报道的来自豌豆叶绿体的一种内肽酶（EP1），通过一个包括超滤、蔗糖梯度离心、等电聚焦和高效液相色谱凝胶过滤的四步方案被纯化了超过11,000倍。该酶被确定为一种金属蛋白酶，需要结合的Zn2+以及添加的Mg2+或Ca2+才能正常发挥活性。当包膜完整时，通过证明其对嗜热菌蛋白酶不敏感，证实了它在豌豆叶绿体基质中的定位。发现了一种攻击EP1的污染性丝氨酸蛋白酶。污染性蛋白酶被4-(2-氨基乙基)-苯磺酰氟抑制，但不被邻菲罗啉抑制，而EP1的敏感性则相反。EP1能够在生理条件下水解天然核酮糖-1,5-二磷酸羧化酶/加氧酶的大亚基。
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本文引用的文献
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Characteristics of ribulose-1,5-bisphosphate carboxylase/oxygenase degradation by lysates of mechanically isolated chloroplasts from wheat leaves.小麦叶片机械分离叶绿体裂解物对1,5-二磷酸核酮糖羧化酶/加氧酶的降解特性
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Thermolysin is a suitable protease for probing the surface of intact pea chloroplasts.嗜热菌蛋白酶是一种用于探测完整豌豆叶绿体表面的合适蛋白酶。
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