Phosphorylation of chicken growth hormone

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 π- 32P-ATP). The extent of phosphorylation was however less than that observed with ovine prolactin. Under the conditi...

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Veröffentlicht in:Life sciences (1973) 1990, Vol.47 (11), p.945-952
Hauptverfasser: Aramburo, C., Donoghue, D., Montiel, J.L., Berghman, L.R., Scanes, C.G.
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container_end_page 952
container_issue 11
container_start_page 945
container_title Life sciences (1973)
container_volume 47
creator Aramburo, C.
Donoghue, D.
Montiel, J.L.
Berghman, L.R.
Scanes, C.G.
description 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 π- 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.
doi_str_mv 10.1016/0024-3205(90)90541-X
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Both native and biosynthetic cGH were phosphorylated by cAMP-dependent protein kinase (and π- 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. 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Psychology</topic><topic>growth hormone</topic><topic>Growth Hormone - metabolism</topic><topic>HORMONES</topic><topic>IMMUNOASSAY</topic><topic>ISOTOPE APPLICATIONS</topic><topic>ISOTOPES</topic><topic>LIGHT NUCLEI</topic><topic>Male</topic><topic>MOLECULAR WEIGHT</topic><topic>NUCLEI</topic><topic>NUCLEOTIDES</topic><topic>ODD-ODD NUCLEI</topic><topic>ORGANIC COMPOUNDS</topic><topic>OXYGEN COMPOUNDS</topic><topic>PEPTIDE HORMONES</topic><topic>PHOSPHATES</topic><topic>PHOSPHORUS 32</topic><topic>PHOSPHORUS COMPOUNDS</topic><topic>PHOSPHORUS ISOTOPES</topic><topic>PHOSPHORUS-GROUP TRANSFERASES</topic><topic>PHOSPHORYLATION</topic><topic>PHOSPHOTRANSFERASES</topic><topic>Pituitary Gland, Anterior - cytology</topic><topic>Pituitary Gland, Anterior - metabolism</topic><topic>PITUITARY HORMONES</topic><topic>Precipitin Tests</topic><topic>Protein hormones. Growth factors. 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Both native and biosynthetic cGH were phosphorylated by cAMP-dependent protein kinase (and π- 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.</abstract><cop>Amsterdam</cop><pub>Elsevier Inc</pub><pmid>2215076</pmid><doi>10.1016/0024-3205(90)90541-X</doi><tpages>8</tpages></addata></record>
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subjects 550501 - Metabolism- Tracer Techniques
AMP
Analytical, structural and metabolic biochemistry
ANIMALS
BASIC BIOLOGICAL SCIENCES
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BIOASSAY
Biological and medical sciences
BIRDS
Cells, Cultured
CHEMICAL REACTIONS
CHICKENS
DAYS LIVING RADIOISOTOPES
Electrophoresis, Polyacrylamide Gel
ENZYMES
FOWL
Fundamental and applied biological sciences. Psychology
growth hormone
Growth Hormone - metabolism
HORMONES
IMMUNOASSAY
ISOTOPE APPLICATIONS
ISOTOPES
LIGHT NUCLEI
Male
MOLECULAR WEIGHT
NUCLEI
NUCLEOTIDES
ODD-ODD NUCLEI
ORGANIC COMPOUNDS
OXYGEN COMPOUNDS
PEPTIDE HORMONES
PHOSPHATES
PHOSPHORUS 32
PHOSPHORUS COMPOUNDS
PHOSPHORUS ISOTOPES
PHOSPHORUS-GROUP TRANSFERASES
PHOSPHORYLATION
PHOSPHOTRANSFERASES
Pituitary Gland, Anterior - cytology
Pituitary Gland, Anterior - metabolism
PITUITARY HORMONES
Precipitin Tests
Protein hormones. Growth factors. Cytokines
Protein Kinases - metabolism
Proteins
RADIOISOTOPES
STH
TRACER TECHNIQUES
TRANSFERASES
VERTEBRATES
title Phosphorylation of chicken growth hormone
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