Phosphorylation of parathyroid hormone by human and bovine parathyroid glands.

作者: S A Rabbani , R Kremer , H P Bennett , D Goltzman

DOI: 10.1016/S0021-9258(17)43241-8

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摘要: Human and bovine parathyroid gland slices were incubated in vitro for varying time periods with inorganic 32P [35S]methionine or [3H]serine. Tissue was then extracted aqueous medium, hormone (PTH) purified. Incorporated found to coelute immunoreactive PTH multiple chromatographic systems, a peak of phosphorylated material could be resolved from the nonphosphorylated by reversed phase high pressure liquid chromatography. The amino acid composition both entities conformed that major glandular species PTH, accounted 10-20% total. A course revealed slow incorporation into hormone, after 4-h preincubation 32P, co-elution its precursor observed. Phosphoserine identified purified labeled Additionally dilute hydrolysis containing generated an 35S-labeled fragment which co-chromatographed. results are consistent phosphorylation on serine residues within NH2-terminal region human glands suggest prohormone occurs as well.

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