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Abstract:

Nuclei isolated from chick embryonic (11-days old) and adult muscles contain 25% and 15%, respectively, of the total cellular protein phosphokinase activity. The specific activity, on a DNA basis, of the adult enzyme is approximaely 4 times lower than that of the nuclei from 11-day-embryos. Nuclear extracts of either stage of development give rise on DEAE cellulose chromatography to two main protein kinase activity peaks, which elute at 20 mm and 300 mm phosphate buffer, pH 7 (protein kinases "A" and "C", respectively). Nuclei of adult muscles contain 10 fold and 3 fold less protein kinases A and C, respectively, than embryonic nuclei. The properties (substrate specificity, effect on activity of NaCl and phosphate, cyclic AMP activability, molecular weight) of protein kinases A and C are different, but those of embryonic and adult protein kinase A or C are indistinguishable, indicating that the transition from nuclei with an active mitosis (embryonic) to a resting state (adult) is accompanied by a quantitative, but not a qualitative, change in the protein kinase pattern. Phosphorylation with [γ-32P] ATP of intact nuclei arising from 11 day and 20 day embryos results in the labelling of histone and nonhistone chromosomal proteins, their specific radioactivity being 2 and 3 times lower, respectively, in the older nuclei than in those from 11 day embryos. © 1977 Dr. W. Junk b.v. Publishers.

Registro:

Documento: Artículo
Título:Nuclear protein phosphokinase activities and phosphorylation of chromosomal proteins in embryonic and adult muscles of the chick
Autor:Piras, M.M.; Piras, R.
Filiación:Instituto de Investigaciones Bioquímicas-F. Campomar, Obligado 2490, Buenos Aires, 1428, Argentina
Palabras clave:cyclic amp; dna; protein kinase; radioisotope; adenosine triphosphate p 32; cell nucleus; chicken; chromosome; embryo; in vitro study; mitosis; muscle; theoretical study; Animal; Cell Nucleus; Chick Embryo; Chickens; Chromosomes; Cytosol; Kinetics; Molecular Weight; Muscles; Nucleoproteins; Protein Kinases; Time Factors
Año:1977
Volumen:16
Número:2-3
Página de inicio:119
Página de fin:125
DOI: http://dx.doi.org/10.1007/BF01732052
Título revista:Molecular and Cellular Biochemistry
Título revista abreviado:Mol Cell Biochem
ISSN:03008177
CODEN:MCBIB
CAS:cyclic AMP, 60-92-4; DNA, 9007-49-2; protein kinase, 9026-43-1; Nucleoproteins; Protein Kinases, EC 2.7.1.37
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v16_n2-3_p119_Piras

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Citas:

---------- APA ----------
Piras, M.M. & Piras, R. (1977) . Nuclear protein phosphokinase activities and phosphorylation of chromosomal proteins in embryonic and adult muscles of the chick. Molecular and Cellular Biochemistry, 16(2-3), 119-125.
http://dx.doi.org/10.1007/BF01732052
---------- CHICAGO ----------
Piras, M.M., Piras, R. "Nuclear protein phosphokinase activities and phosphorylation of chromosomal proteins in embryonic and adult muscles of the chick" . Molecular and Cellular Biochemistry 16, no. 2-3 (1977) : 119-125.
http://dx.doi.org/10.1007/BF01732052
---------- MLA ----------
Piras, M.M., Piras, R. "Nuclear protein phosphokinase activities and phosphorylation of chromosomal proteins in embryonic and adult muscles of the chick" . Molecular and Cellular Biochemistry, vol. 16, no. 2-3, 1977, pp. 119-125.
http://dx.doi.org/10.1007/BF01732052
---------- VANCOUVER ----------
Piras, M.M., Piras, R. Nuclear protein phosphokinase activities and phosphorylation of chromosomal proteins in embryonic and adult muscles of the chick. Mol Cell Biochem. 1977;16(2-3):119-125.
http://dx.doi.org/10.1007/BF01732052