Schleyer M, Voigt K H
Hoppe Seylers Z Physiol Chem. 1979 Oct;360(10):1473-81. doi: 10.1515/bchm2.1979.360.2.1473.
A recently published method for preparation of porcine growth hormone resulted in a highly purified protein with good biological activity. However, after storing for some months the originally homogeneous hormone separated again into several fractions when rechromatographed on ion exchange columns. The biological activity, found in one of these fractions, was clearly diminished compared with the activity of a freshly prepared hormone. In the present paper a modified procedure is described for the isolation of a more stable porcine growth hormone. The influence of ions, involved in buffers of the same molarity and the same pH, upon ion exchange chromatography of porcine growth hormone is discussed. The purified hormone shows high biological activity in the tibia test and is free of activities of other pituitary hormones. The molecular weight is about 20 000; only phenylalanine is found as N-terminal as well as C-terminal amino acid; the amino acid composition resembles neither that of porcine growth hormone described in literature nor that of human growth hormone.
最近发表的一种制备猪生长激素的方法得到了一种具有良好生物活性的高度纯化蛋白质。然而，储存几个月后，当在离子交换柱上重新进行色谱分析时，原本均一的激素又再次分离成几个组分。在这些组分中的一种中发现的生物活性与新制备的激素活性相比明显降低。在本文中，描述了一种改进的程序，用于分离更稳定的猪生长激素。讨论了相同摩尔浓度和相同pH值的缓冲液中所含离子对猪生长激素离子交换色谱的影响。纯化的激素在胫骨试验中显示出高生物活性，并且没有其他垂体激素的活性。其分子量约为20000；仅发现苯丙氨酸作为N末端和C末端氨基酸；其氨基酸组成既不像文献中描述的猪生长激素，也不像人生长激素。
