Phosphorylation of chicken growth hormone. Academic Article

abstract

• The possibility that chicken growth hormone (cGH) can be phosphorylated has been examined. Both native and biosynthetic cGH were phosphorylated by cAMP-dependent protein kinase (and gamma -32P-ATP). The extent of phosphorylation was however less than that observed with ovine prolactin. Under the conditions employed, glycosylated cGH was not phosphorylated. Chicken anterior pituitary cells in primary culture were incubated in the presence of 32P-phosphate. Radioactive phosphate was incorporated in vitro into the fraction immunoprecipitable with antisera against cGH. Incorporation was increased with cell number and time of incubation. The presence of GH releasing factor (GRF) increased the release of 32P-phosphate labelled immunoprecipitable GH into the incubation media but not content of immunoprecipitable GH in the cells. The molecular weight of the phosphorylated immunoreactive cGH in the cells corresponded to cGH dimer.

authors

• Berghman, Luc

published proceedings

• Life Sci

author list (cited authors)

• Aramburo, C., Donoghue, D., Montiel, J. L., Berghman, L. R., & Scanes, C. G.

citation count

• 15

complete list of authors

• Aramburo, C||Donoghue, D||Montiel, JL||Berghman, LR||Scanes, CG

publication date

• January 1990

publisher

• Elsevier  Publisher

published in

• LIFE SCIENCES  Journal

keywords

• Animals
• Cells, Cultured
• Chickens
• Electrophoresis, Polyacrylamide Gel
• Growth Hormone
• Male
• Phosphorylation
• Pituitary Gland, Anterior
• Precipitin Tests
• Protein Kinases

PubMed Central ID

• 2215076

Digital Object Identifier (DOI)

• 10.1016/0024-3205(90)90541-x

start page

• 945

end page

• 952

volume

• 47

issue

• 11

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2F0024-3205%2890%2990541-x