STRUCTURE-FUNCTION-RELATIONSHIPS IN GLUCAGON - PROPERTIES OF HIGHLY PURIFIED DES-HIS1-, MONOIODO-, AND [DES-ASN28,THR29](HOMOSERINE LACTONE27)-GLUCAGON
STRUCTURE-FUNCTION-RELATIONSHIPS IN GLUCAGON - PROPERTIES OF HIGHLY PURIFIED DES-HIS1-, MONOIODO-, AND [DES-ASN28,THR29](HOMOSERINE LACTONE27)-GLUCAGON
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DOI：
10.1021/bi00679a002
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发表时间：
1975-01-01
期刊：
影响因子：
2.9
通讯作者：
RODBELL, M
中科院分区：
文献类型：
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作者：
LIN, MC;WRIGHT, DE;RODBELL, M
我们比较了胰高血糖素和三种高度纯化的胰高血糖素衍生物激活肝腺苷酸环化酶（表达该激素的生物活性）和与胰高血糖素竞争结合肝质膜胰高血糖素特异性位点的能力。相对于胰高血糖素，通过CNBr处理胰高血糖素制备的[des-Asn 28，Thr 29]（高丝氨酸内酯27）-胰高血糖素的生物活性和亲和力同样降低40- 50倍。相比之下，通过不溶性Edman试剂制备并高度纯化（天然胰高血糖素污染小于0.5%）的des-His '-胰高血糖素显示出亲和力降低15倍，但生物活性相对于天然激素降低50倍。在最大刺激浓度下，导致激素反应的级联反应中的第一个事件是激素与其称为“受体”的识别位点的相互作用。一般认为，激素与受体的结合引起反应系统的某些变化。对激素识别和作用的结构要求的研究应该提供对激素作用机制的进一步理解。
We have compared the ability of glucagon and three highly purified derivatives of the hormone to activate hepatic adenylate cyclase (an expression of biologicalactiv-ity of the hormone) and to compete with [125] glucagon for binding to sites specificfor glucagon in hepatic plasma membranes. Relative to that of glucagon, biological activity and affinity of [des-Asn28, Thr29](homoserine lactone27)-glucagon, prepared by CNBr treatment of glucagon, were reduced equally by 40-to 50-fold. By contrast, des-His’-glucagon, prepared by an insoluble Edman reagent and highly purified (less than 0.5% contamination with native glucagon), displayed a 15-fold decrease in affinity but a 50-fold decrease in biological activity relative to that of the native hormone. At maximal stimulating concentrations, X he first event in the cascade of reactions leading to hor-mone response is the interaction of the hormone with its recognition site termed the “receptor”. It is commonly as-sumed that binding of the hormone to the receptor induces certain transformations in the responding system. Studies of the structural requirements for hormonal recognition and action should provide further understanding of the mechanism of hormone action.