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:
影响因子:
--
通讯作者:
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
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.