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人垂体生长激素:纤溶酶消化产物中两个生物活性片段的分离与特性

Human pituitary growth hormone: isolation and properties of two biologically active fragments from plasmin digests.

作者信息

Li C H, Gráf L

出版信息

Proc Natl Acad Sci U S A. 1974 Apr;71(4):1197-201. doi: 10.1073/pnas.71.4.1197.

Abstract

Two biologically active fragments have been isolated from plasmic digests of human pituitary growth hormone. It was shown that these two fragments were derived from the cleavage of the Arg-Thr (positions 134-135) and the Lys-Gln (positions 140-141) bonds of the hormone: one has 134 amino acids and the other 51 amino acids, respectively. The two fragments were active in the rat tibia and pigeon crop-sac tests, as well as in complement fixation experiments.

摘要

已从人垂体生长激素的血浆消化物中分离出两个生物活性片段。结果表明,这两个片段分别源自该激素的精氨酸 - 苏氨酸(第134 - 135位)和赖氨酸 - 谷氨酰胺(第140 - 141位)键的断裂:一个片段有134个氨基酸,另一个有51个氨基酸。这两个片段在大鼠胫骨和鸽嗉囊试验以及补体结合实验中均具有活性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/fb2c/388191/a7f2bcae1a05/pnas00057-0191-a.jpg

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