Radioiodination of microgram quantities of ribosomal proteins from polyacrylamide gels

A method has been developed for radiolabeling small amounts of ribosomal proteins extracted from polyacrylamide gels with potassium [ 125]Iiodide. The procedure was used to label even those proteins which lack tyrosine and histidine residues by the modification of proteins with methyl p-hydroxybenzi...

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Veröffentlicht in:	Analytical biochemistry 1980-03, Vol.103 (1), p.101-109
Hauptverfasser:	Tolan, Dean R., Lambert, John M., Boileau, Guy, Fanning, Thomas G., Kenny, James W., Vassos, Artemios, Traut, Robert R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Electrophoresis, Polyacrylamide Gel - methods Escherichia coli - analysis Histidine Iodine Radioisotopes Isotope Labeling - methods Microchemistry - methods Rabbits Reticulocytes - analysis Ribosomal Proteins - analysis Ribosomal Proteins - isolation & purification Tyrosine
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Beschreibung
Zusammenfassung:	A method has been developed for radiolabeling small amounts of ribosomal proteins extracted from polyacrylamide gels with potassium [ 125]Iiodide. The procedure was used to label even those proteins which lack tyrosine and histidine residues by the modification of proteins with methyl p-hydroxybenzimidate. Specific radioactivities obtained range from 20,000 to 200,000 cpm/μg. The method has been used in the identification of eukaryotic ribosomal proteins from rabbit reticulocytes separated by polyacrylamide/sodium dodecyl sulfate gel electrophoresis.
ISSN:	0003-2697 1096-0309
DOI:	10.1016/0003-2697(80)90243-2