Identification of gamma-glutamyl phosphate in the alpha 2 chains of chicken bone collagen.
- 1 September 1979
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 76 (9) , 4327-4330
- https://doi.org/10.1073/pnas.76.9.4327
Abstract
Purified components of chicken bone collagen contain approximately 4 atoms of organic P/mol of collagen, located principally in the .alpha.2 chains. Tritiated .alpha.-amino-.delta.-hydroxyvaleric acid was isolated after reductive cleavage with NaB[3H]H4 of the .gamma. components, the .alpha.2 chains and peptides enriched in organic phosphorus derived from the .alpha.2 chains. Tritiated .alpha.-amino-.delta.-hydroxyvaleric acid was not detected in any of the following unphosphorylated proteins after cleavage with NaB[3H]H4: albumin and lysozyme, the .alpha.2 chains of several unmineralized tissues and, most importantly, dephosphorylated .alpha.2 chains of chicken bone collagen. Chicken bone collagen contains .gamma.-glutamyl phosphate. The .alpha.2 chain of chicken bone collagen is the 1st structural protein containing an acyl phosphate.Keywords
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