Isolation and characterization of the bioactive circulating human parathyroid hormone, hPTH-1-37

被引:20
作者
Hock, D
Magerlein, M
Heine, G
Ochlich, PP
Forssmann, WG
机构
[1] NIEDERSACHS INST PEPTIDE FORSCH, D-30625 HANNOVER, GERMANY
[2] BOEHRINGER MANNHEIM GMBH, D-68305 MANNHEIM, GERMANY
来源
FEBS LETTERS | 1997年 / 400卷 / 02期
基金
中国国家自然科学基金; 上海市自然科学基金;
关键词
parathyroid hormone; isolation; hemofiltrate; dialysis; human;
D O I
10.1016/S0014-5793(96)01390-7
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 clear-cut increase in serum calcium concentration, We conclude that hPTH-1-37 is the native bioactive fragment of hPTH-1-84 in circulation.
引用
收藏
页码:221 / 225
页数:5
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