Dib R, Chobert J M, Dalgalarrondo M, Barbier G, Haertlé T
Institut National de la Recherche Agronomique, Laboratoire d'Etude des Interactions des Molécules Alimentaires, Nantes, France.
FEBS Lett. 1998 Jul 17;431(2):279-84. doi: 10.1016/s0014-5793(98)00782-0.
A protease was isolated and purified from the supernatant of a culture of hyperthermophilic archaebacteria: Pyrococcus abyssi strain st 549. Purification consisted of three chromatographic steps. The enzyme purification yield was 4% and the purification factor 890. This protease is a seryl-protease hydrolyzing proteins and peptides with a preference for cleavage at the aromatic and hydrophobic residues in P1 and P'1 positions. Its activity is optimal at 95 degrees C and at pH 9. The electrophoretic mobility of the protease observed by zymogram suggests that it can adopt several oligomer forms. Three of them predominate displaying apparent molecular masses of 150, 105 and 60 kDa. Interdependence of the observed bands was revealed by changing the denaturation conditions of the samples (temperature, SDS concentration) before electrophoresis.
从嗜热古细菌深渊嗜热栖热菌（Pyrococcus abyssi）菌株st 549培养物的上清液中分离并纯化了一种蛋白酶。纯化过程包括三个色谱步骤。酶的纯化产率为4%，纯化因子为890。这种蛋白酶是一种丝氨酸蛋白酶，可水解蛋白质和肽，优先在P1和P'1位置的芳香族和疏水性残基处切割。其活性在95℃和pH 9时最佳。通过酶谱观察到的蛋白酶的电泳迁移率表明它可以呈现几种寡聚体形式。其中三种占主导，表观分子量分别为150、105和60 kDa。通过改变电泳前样品的变性条件（温度、SDS浓度）揭示了观察到的条带之间的相互依赖性。
