Nikolaidis M N, Parsadanian A Sh, Pozmogova G E, El'darov M A, Anan'eva N M, Maĭsurian N A, Galoian A A
Mol Biol (Mosk). 1994 Sep-Oct;28(5):1098-105.
A recombinant plasmid providing for the synthesis and secretion of the human atrial natriuretic peptide (hANP) as a C-terminal hybrid with the St. aureus protein A was constructed. The level of secretion of the chimeric proteins and their proteolytic stability were shown to depend upon the genotype of the recipient strains and the cultivation conditions. The hybrid proteins were purified by chromatography on IgG Sepharose. The presence of peptides corresponding to the hANP in the acid hydrolysates of the secreted and affinity-purified proteins was confirmed by the enzyme-linked immunoassay and analytical HPLC.
构建了一种重组质粒，用于合成和分泌作为与金黄色葡萄球菌蛋白A的C末端杂合体的人心房钠尿肽（hANP）。已表明嵌合蛋白的分泌水平及其蛋白水解稳定性取决于受体菌株的基因型和培养条件。通过IgG Sepharose柱层析法纯化杂合蛋白。通过酶联免疫测定和分析型高效液相色谱法证实了分泌的和亲和纯化的蛋白的酸水解产物中存在与hANP相对应的肽段。
