Thymocyte growth peptide (TGP) promotes DNA synthesis of immature thymocytes. TGP has been purified from sheep, human and calf thymus and recently characterized as an N-terminally blocked nonapeptide. Evidence is presented here that the blocking moiety consists of a formylpteroyl group bound to the N-terminal glutamyl residue of the nonapeptide. The pterin part of the TGP molecule has a ribityl substituent in analogy with riboflavin, which explains the pronounced hydrophilic property of TGP in contrast to unsubstituted and unconjugated folates. The compound can be classified as a ribofolate peptide, a novel class of growth factor. Zn2+ counteracts degradation of the molecule and is required for full biological activity; mass spectrometric data confirm that native TGP contains zinc.
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April 01 1991
Identification of a mammalian growth factor as a ribofolate peptide
Ulf Ernström
Ulf Ernström
1Department of Histology and Neurobiology, Karolinska Institutet, Box 60 400, S-104 01 Stockholm, Sweden
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Publisher: Portland Press Ltd
Received:
April 05 1991
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1991 Plenum Publishing Corporation
1991
Biosci Rep (1991) 11 (2): 119–130.
Article history
Received:
April 05 1991
Citation
Ulf Ernström; Identification of a mammalian growth factor as a ribofolate peptide. Biosci Rep 1 April 1991; 11 (2): 119–130. doi: https://doi.org/10.1007/BF01119199
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