Phosphorylation of a 25,000-dalton protein in slow and fast muscles of the chicken.
Protein phosphorylation in intact chicken latissimus dorsi muscle, slow anterior (ALD) and fast posterior (PLD), was compared. A major difference in [32P]phosphate incorporation was found between the ALD and PLD in a 25,000-dalton heat soluble protein. The 25,000-dalton protein was purified from both the ALD and PLD. The two proteins had similar amino acid composition and both contained approximately 1 mole phosphate per mole of protein. The difference in their content of radioactive phosphate was determined to be due to faster turnover in the ALD.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D008297:Male; D008970:Molecular Weight; D009124:Muscle Proteins / Q000302:isolation & purification / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation
D000596:Amino Acids; D009124:Muscle Proteins; D010710:Phosphates; D010750:Phosphoproteins