Isolation, structure and synthesis of a heptapeptide with in vitro ACTH-releasing activity from porcine hypothalamus.

Isolation, structure and synthesis of a heptapeptide with in vitro ACTH-releasing activity from porcine hypothalamus.
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猪下丘脑具有体外 ACTH 释放活性的七肽的分离、结构和合成。

DOI:
10.1055/s-2007-1019228
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发表时间:
1981
期刊:
Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme
影响因子:
--
通讯作者:
Schally,AV
Schally,AV
中科院分区:
--
文献类型:
--
作者:
Chang,RC;Huang,WY;Arimura,A;Redding,TW;Coy,DH;Saffran,M;Kong,A;Hamilton,JW;Cohn,DV;Schally,AV

文献摘要

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猪下丘脑酸性提取物经SephadexG-25凝胶过滤得到Rf = 0.82-0.7或VE/VT = 0.41-0.48的组分,其CRF活性显著。在随后的纯化过程中,特别是在最后两个步骤中,该馏分的活性显著降低。从该组分中分离得到一个具有促肾上腺皮质激素释放活性的七肽,其氨基酸序列为H-Phe-Ile-Tyr-His-Ser-Tyr-Lys-OH。用固相法合成了该七肽。体外合成七肽的CRF活性较低,但可通过大鼠下丘脑提取物中的辅因子组分增强。
Significant CRF activity was found in a fraction with R f= 0.82-0.7 or V E/V T= 0.41-0.48 obtained by gel filtration of acid extracts of pig hypothalami on Sephadex G-25. The activity of this fraction decreased markedly during subsequent purification, particularly in the last two steps. From this fraction, a heptapeptide with significant ACTH releasing activity in vitro, was isolated in pure state, and its amino acid sequence was established as H-Phe-Ile-Tyr-His-Ser-Tyr-Lys-OH. This heptapeptide was synthesized by solid phase methods. The CRF activity of synthetic heptapeptide in vitro was low but could be potentiated by a cofactor fraction from rat hypothalamic extract.