Human growth hormone: Difference between revisions
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HGH is phosphorylated on Ser residues 132 and 176 (Giorgianni, Beranova-Giorgianni, and Desiderio, 2004)<ref>PMID:14997482</ref>. Other research has indicated possible phosphorylation of Tyr residues 35 and 42. However, these phosphorylations were only investigated in carcinoma cells with constitutively active epidermal growth factor-stimulated tyrosine kinase (Baldwin et al., 1983)<ref>PMID:6600511</ref>. The overall influence of these post-translational modifications on hGH activity has yet to be determined. | HGH is phosphorylated on Ser residues 132 and 176 (Giorgianni, Beranova-Giorgianni, and Desiderio, 2004)<ref>PMID:14997482</ref>. Other research has indicated possible phosphorylation of Tyr residues 35 and 42. However, these phosphorylations were only investigated in carcinoma cells with constitutively active epidermal growth factor-stimulated tyrosine kinase (Baldwin et al., 1983)<ref>PMID:6600511</ref>. The overall influence of these post-translational modifications on hGH activity has yet to be determined. | ||
==Receptor Binding Site== | ==Receptor Binding Site== |