Human pituitary growth hormone

isolation and properties of two biologically active fragments from plasmin digests

C. H. Li, L. Gráf

Research output: Contribution to journalArticle

72 Citations (Scopus)

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 l40 l41) 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.

Original languageEnglish
Pages (from-to)1197-1201
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume71
Issue number4
Publication statusPublished - 1974

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Human Growth Hormone
Fibrinolysin
Growth Hormone
Amino Acids
Columbidae
Tibia
Hormones

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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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 l40 l41) 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.",
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AB - 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 l40 l41) 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.

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