Abstract
1. 1. Exogenous and endogenous tyrosine protein phosphorylation activities were examined in soluble and partieulate fractions from various normal tissues by using poly-[Glu- 80Na, Tyr 20] and a monoclonal antibody specific for phosphotyrosine. 2. 2. Phosphorylation of the exogenous substrate by the partieulate forms of TPKs was 2- to 10-fold higher than by soluble forms. The activities of partieulate and soluble enzymes decreased in the following order: spleen > (thymus = kidney) > testes ⩾ (pancreas = liver = brain) > heart. 3. 3. The level of endogenous phosphorylation in the tissues decreased respectively in the following order: thymus > brain ⩾ (pancreas = liver) > spleen > testes > kidney > heart for the partieulate fractions, and spleen > thymus > brain > pancreas ⩾ liver > testes > kidney > heart for the soluble fractions. 4. 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.
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