Two contiguous thrombin fragments of human somatotropin form a functionally active recombinant, but the two homologous fragments from sheep hormone do not

L. Gráf, Choh Hao Li, Christopher H K Cheng, Michael D. Jibson

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Two thrombin fragments of reduced-carbamidomethylated human somatotropin representing the full primary structure of the native hormone (residues 1-134 and 135-191) have been found to form a recombinant molecule with properties similar to those of reduced-carbamidomethylated human somatotropin as shown by circular dichroism spectroscopy, two receptor-binding assays, and radioimmunoassay. In contrast, the homologous thrombin fragments of reduced-carbamido-methylated sheep hormone (residues 1-133 and 134-191) do not undergo recombination. Furthermore, neither the reduced-alkylated nor the reduced and nonalkylated C-terminal thrombin fragment of sheep hormone is able to interact with the reduced-carbamidomethylated N-terminal thrombin fragment of human hormone, under conditions which favor the recombination of the two human somatotropin fragments.

Original languageEnglish
Pages (from-to)7251-7258
Number of pages8
JournalBiochemistry
Volume20
Issue number25
Publication statusPublished - 1981

Fingerprint

Human Growth Hormone
Thrombin
Sheep
Hormones
Genetic Recombination
Circular dichroism spectroscopy
Circular Dichroism
Radioimmunoassay
Assays
Spectrum Analysis
Molecules

ASJC Scopus subject areas

  • Biochemistry

Cite this

Two contiguous thrombin fragments of human somatotropin form a functionally active recombinant, but the two homologous fragments from sheep hormone do not. / Gráf, L.; Li, Choh Hao; Cheng, Christopher H K; Jibson, Michael D.

In: Biochemistry, Vol. 20, No. 25, 1981, p. 7251-7258.

Research output: Contribution to journalArticle

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