Preparation of a specifically tritiated locust adipokinetic hormone analog with full biological potency.
Preparation of a specifically tritiated locust adipokinetic hormone analog with full biological potency.
复制标题
具有完全生物效力的特异性氚化蝗虫脂肪运动激素类似物的制备。
DOI：
10.1111/j.1399-3011.1984.tb02743.x
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
Applebaum,SW
中科院分区：
文献类型：
--
作者：
Muramoto,K;Ramachandran,J;Moshitzky,P;Applebaum,SW
将含有酪氨酸残基代替苯丙氨酸的脂肪动力学激素（AKH）和虾红色素浓缩激素（RPCH）相关合成肽碘化，并通过反相HPLC分离3，5-二碘酪氨酰衍生物。在氚的存在下，二碘衍生物的催化脱卤产生了氚化AKH类似物，通过Sephadex LH-20凝胶过滤和反相HPLC进行分离。氚标记的肽被形成为与AKH在其刺激脂质释放到蝗虫体内血淋巴中的能力相同，其中二碘色糖基衍生物是无活性的。氚化肽的比放射性为57.2 Ci/mmol，或理论值的99%。
A synthetic peptide related to locus adipokinetic hormone (AKH) and shrimp red pigment concentrating hormone (RPCH) containing a tyrosine residue in place of phenylalanine was iodinated and the 3,5‐diiodotyrosyl derivative was isolated by reverse phase HPLC. Catalytic dehalogenation of the diiodo derivative in the presence of tritium yielded the tritiated AKH analog which was isolated by gel filtration on Sephadex LH‐20 and reverse phase HPLC. The tritiated peptide was formed to be identical to AKH in its ability to stimulate lipid release into the hemolymph of locustsin vivowhere the diiodotryrosyl derivative was inactive. The specific radioactivity of the tritiated peptide was 57.2 Ci/mmol, or 99% of the theoretical value.