Human somatotropin

Covalent reconstitution of two polypeptide contiguous fragments with thrombin

L. Gráf, C. H. Li

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Thrombin has been shown to resynthesize the Arg135 peptide bond between the 134- and 57-residue thrombin fragments of reduced and carbamidomethylated human somatotropin at pH 6.0 in 90% (vol/vol) glycerol. The maximal amount of synthesis was about 20% as estimated by sodium dodecyl sulfate gel electrophoresis and radioreceptor assay. The resynthesized polypeptide was isolated and shown to be indistinguishable from the reduced and carbamidomethylated hormone when tested by two receptor-binding assays, radioimmunoassay, and rat tibia test.

Original languageEnglish
Pages (from-to)6135-6138
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume78
Issue number10 I
Publication statusPublished - 1981

Fingerprint

Human Growth Hormone
Thrombin
Radioligand Assay
Peptides
Tibia
Sodium Dodecyl Sulfate
Glycerol
Radioimmunoassay
Electrophoresis
Gels
Hormones

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

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abstract = "Thrombin has been shown to resynthesize the Arg135 peptide bond between the 134- and 57-residue thrombin fragments of reduced and carbamidomethylated human somatotropin at pH 6.0 in 90{\%} (vol/vol) glycerol. The maximal amount of synthesis was about 20{\%} as estimated by sodium dodecyl sulfate gel electrophoresis and radioreceptor assay. The resynthesized polypeptide was isolated and shown to be indistinguishable from the reduced and carbamidomethylated hormone when tested by two receptor-binding assays, radioimmunoassay, and rat tibia test.",
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journal = "Proceedings of the National Academy of Sciences of the United States of America",
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T1 - Human somatotropin

T2 - Covalent reconstitution of two polypeptide contiguous fragments with thrombin

AU - Gráf, L.

AU - Li, C. H.

PY - 1981

Y1 - 1981

N2 - Thrombin has been shown to resynthesize the Arg135 peptide bond between the 134- and 57-residue thrombin fragments of reduced and carbamidomethylated human somatotropin at pH 6.0 in 90% (vol/vol) glycerol. The maximal amount of synthesis was about 20% as estimated by sodium dodecyl sulfate gel electrophoresis and radioreceptor assay. The resynthesized polypeptide was isolated and shown to be indistinguishable from the reduced and carbamidomethylated hormone when tested by two receptor-binding assays, radioimmunoassay, and rat tibia test.

AB - Thrombin has been shown to resynthesize the Arg135 peptide bond between the 134- and 57-residue thrombin fragments of reduced and carbamidomethylated human somatotropin at pH 6.0 in 90% (vol/vol) glycerol. The maximal amount of synthesis was about 20% as estimated by sodium dodecyl sulfate gel electrophoresis and radioreceptor assay. The resynthesized polypeptide was isolated and shown to be indistinguishable from the reduced and carbamidomethylated hormone when tested by two receptor-binding assays, radioimmunoassay, and rat tibia test.

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M3 - Article

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JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

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IS - 10 I

ER -