Protein tyrosine phosphorylation in normal rat tissues.
1. Exogenous and endogenous tyrosine protein phosphorylation activities were examined in soluble and particulate fractions from various normal tissues by using poly-[Glu-80Na, Tyr20] and a monoclonal antibody specific for phosphotyrosine. 2. Phosphorylation of the exogenous substrate by the particulate forms of TPKs was 2- to 10-fold higher than by soluble forms. The activities of particulate and soluble enzymes decreased in the following order: spleen > (thymus = kidney) > testes > or = (pancreas = liver = brain) > heart. 3. The level of endogenous phosphorylation in the tissues decreased respectively in the following order: thymus > brain > or = (pancreas = liver) > spleen > testes > kidney > heart for the particulate fractions, and spleen > thymus > brain > pancreas > or = liver > testes > kidney > heart for the soluble fractions. 4. A large number of phosphotyrosine-containing proteins were detected. In addition, several phosphotyrosine-containing proteins of similar molecular weight were found in different tissues and fractions.
Tremblay
L
L
Laboratoire de Membranologie, Université du Québec à Montréal, Canada.
Beliveau
R
R
D000595:Amino Acid Sequence; D000818:Animals; D008297:Male; D008969:Molecular Sequence Data; D009928:Organ Specificity / Q000502:physiology; D010766:Phosphorylation; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D012016:Reference Values; D012995:Solubility; D014018:Tissue Distribution
D011505:Protein-Tyrosine Kinases