Benlot C, Antreassian J, Henry J P, Legrand J C, Gros F, Thibault J
Biochimie. 1985 Jun;67(6):589-95. doi: 10.1016/s0300-9084(85)80198-x.
mRNAs extracted from human pheochromocytoma were translated in vitro in a lysate of a rabbit reticulocytes. Two enzymes of the biosynthetic pathway of the catecholamines, tyrosine-hydroxylase (TH) and dopamine-beta-hydroxylase (DBH), were characterized as translation products after immunoprecipitation by specific antisera and electrophoretic analysis. The precursor of TH is a polypeptide having a molecular mass of 62,000 identical to that found for the mature protein. The molecular mass of the precursor of DBH 73,000 while that of the mature form is 79,000. TH and DBH have been translated from mRNAs having sedimentation coefficients of 22S and 25S, respectively.
从人嗜铬细胞瘤中提取的mRNA在兔网织红细胞裂解物中进行体外翻译。儿茶酚胺生物合成途径中的两种酶,酪氨酸羟化酶(TH)和多巴胺β羟化酶(DBH),经特异性抗血清免疫沉淀和电泳分析后被鉴定为翻译产物。TH的前体是一种分子量为62,000的多肽,与成熟蛋白的分子量相同。DBH前体的分子量为73,000,而成熟形式的分子量为79,000。TH和DBH分别从沉降系数为22S和25S的mRNA翻译而来。