Thorpe D S, Niu S, Morkin E
University Heart Center, University of Arizona College of Medicine, Tucson 85724.
Biochem Biophys Res Commun. 1991 Oct 31;180(2):538-44. doi: 10.1016/s0006-291x(05)81098-8.
Using a bacterial expression system, large amounts of the catalytic core of an atrial natriuretic peptide receptor guanylyl cyclase were produced and purified. After refolding the protein from a buffer containing urea, the enzyme had positively cooperative kinetics with a Hill coefficient, nH = 1.42 +/- 0.08. Size exclusion chromatography and denaturing polyacrylamide gel electrophoresis demonstrated that the enzyme is composed of homodimers with interacting catalytic sites.
利用细菌表达系统,大量生产并纯化了心房利钠肽受体鸟苷酸环化酶的催化核心。在从含有尿素的缓冲液中对该蛋白进行重折叠后,该酶具有正协同动力学,希尔系数(nH = 1.42 ± 0.08)。尺寸排阻色谱法和变性聚丙烯酰胺凝胶电泳表明,该酶由具有相互作用催化位点的同型二聚体组成。