人甲状旁腺激素1-34 N端合成片段对牛和猪肾膜的体外比较生物学活性

Comparative in vitro biological activity of 1-34 N-terminal synthetic fragments of human parathyroid hormone on bovine and porcine kidney membranes.

作者信息

Bader C A, Monet J D, Rivaille P, Gaubert C M, Moukhtar M S, Milhaud G, Funck-Brentano J L

出版信息

Endocr Res Commun. 1976;3(3-4):167-86. doi: 10.3109/07435807609056898.

Abstract

1-34 N-terminal fragments of human parathyroid hormone with sequences according to Brewer et al (hPTHB) and to Niall et al (hPTHN) were synthesized and compared for their ability to activate bovine and porcine kidney cortex membrane adenylate cyclase. Results show that these two hormone sequences are able to activate these membranes but at least in this in vitro assay, hPTHN is about 10 times more active than hPTHB on bovine as well as on porcine membranes. These "apparent potencies" with respect to the potency of bPTH 1-34 in bovine and porcine membrane assay systems are respectively 4% and 11% for hPTHB and 39% and 156% for hPTHN. These relative potencies may be interpreted as corresponding to species specificity of the hormone receptor structural relationships.

摘要

合成了具有布鲁尔等人（hPTHB）和尼尔等人（hPTHN）所描述序列的人甲状旁腺激素1 - 34 N端片段，并比较了它们激活牛和猪肾皮质膜腺苷酸环化酶的能力。结果表明，这两种激素序列都能够激活这些膜，但至少在这种体外试验中，hPTHN在牛和猪的膜上的活性比hPTHB高约10倍。在牛和猪膜检测系统中，相对于bPTH 1 - 34的效力，hPTHB的这些“表观效力”分别为4%和11%，hPTHN为39%和156%。这些相对效力可解释为对应于激素受体结构关系的物种特异性。