Hock D, Mägerlein M, Heine G, Ochlich P P, Forssmann W G
Niedersächsisches Institut für Peptid-Forschung (IPF), Hannover, Germany.
FEBS Lett. 1997 Jan 3;400(2):221-5. doi: 10.1016/s0014-5793(96)01390-7.
The occurrence of hPTH-1-37 as the native bioactive circulating form of PTH-1-84 has now been obtained using a specific purification procedure for circulating parathyroid hormone, which involves a newly developed immunoenzymetric assay for N-terminally intact hPTH. In combination with two different methods of mass spectrometry, the molecular weight of the isolated immunoreactive peptide was shown to be 4401 Da, which corresponds to hPTH-1-37. Synthetic hPTH-1-37 material was tested in the chick bioassay and produced a clearcut increase in serum calcium concentration. We conclude that hPTH-1-37 is the native bioactive fragment of hPTH-1-84 in circulation.
通过一种针对循环甲状旁腺激素的特定纯化程序,现已获得了hPTH-1-37作为PTH-1-84天然生物活性循环形式的结果。该程序涉及一种新开发的针对N端完整hPTH的免疫酶测定法。结合两种不同的质谱方法,分离出的免疫反应性肽的分子量显示为4401 Da,这与hPTH-1-37相对应。合成的hPTH-1-37物质在雏鸡生物测定中进行了测试,并使血清钙浓度明显升高。我们得出结论,hPTH-1-37是循环中hPTH-1-84的天然生物活性片段。