Reyes L B, Scopes R K
Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia.
Bioseparation. 1991;2(3):137-46.
The purification of detergent-solubilized membrane-bound phosphatases from Zymomonas mobilis using novel adsorbents is described. The prepared adsorbents have a hydrophobic core with functional groups attached. These functional groups may either increase or decrease the hydrophobicity of the adsorbent, or participate in other forms of interactions. Adsorption of acid phosphatase (ACP), alkaline phosphatase (ALP) and ATPase to these adsorbents was salt-promoted. Desorption was achieved by decreasing the salt concentration or by displacement with increasing concentration of Triton X-100. The results indicate that chromatography on multifunctional adsorbents that are predominantly hydrophobic in character is a procedure that can have a general applicability in purification of membrane proteins.
本文描述了使用新型吸附剂从运动发酵单胞菌中纯化去污剂增溶的膜结合磷酸酶的方法。所制备的吸附剂具有附着官能团的疏水核心。这些官能团可增加或降低吸附剂的疏水性,或参与其他形式的相互作用。酸性磷酸酶(ACP)、碱性磷酸酶(ALP)和ATP酶对这些吸附剂的吸附受到盐的促进。通过降低盐浓度或用浓度不断增加的 Triton X-100进行置换来实现解吸。结果表明,基于主要具有疏水特性的多功能吸附剂的色谱法是一种可普遍应用于膜蛋白纯化的方法。