App C, Knop J, Huff T, Sticht H, Hannappel E (2013)
Publication Type: Journal article
Publication year: 2013
Publisher: Springer Verlag (Germany)
Book Volume: 32
Pages Range: 484-92
Journal Issue: 6
DOI: 10.1007/s10930-013-9507-0
Thymosin ?4 is the prototype of ?-thymosins and is present in almost every mammalian cell. It is regarded to be the main intracellular G-actin sequestering peptide. Thymosin ?4 serves as a specific glutaminyl substrate for guinea pig transglutaminase. In the absence of an appropriate additional aminyl donor an ?-amino group of thymosin ?4 serves also as an aminyl substrate and an intramolecular bond is formed concomitantly NH3 (17 Da) is lost. The molecular mass of the product is 4,949.6 Da. This is 16.3 Da less than the molecular mass of thymosin ?4 (4,965.9 Da). Digestion with endopeptidases and Edman degradation of the fragments identified the exact position of the ring forming isopeptide bond. In spite of 3 glutaminyl and 9 lysyl residues of thymosin ?4 only one isopeptide bond between Lys16 and Gln36 was formed (cyclic thymosin ?4). These two amino acid residues are conserved in all ?-thymosins. Cyclic thymosin ?4 still forms a complex with G-actin albeit the stability of the complex is about one fiftieth of the stability of the thymosin ?4 × G-actin complex.
APA:
App, C., Knop, J., Huff, T., Sticht, H., & Hannappel, E. (2013). Thymosin ?4 and tissue transglutaminase. Molecular characterization of cyclic thymosin ?4. Protein Journal, 32(6), 484-92. https://doi.org/10.1007/s10930-013-9507-0
MLA:
App, Christine, et al. "Thymosin ?4 and tissue transglutaminase. Molecular characterization of cyclic thymosin ?4." Protein Journal 32.6 (2013): 484-92.
BibTeX: Download