Gates R E, King L E
Department of Medicine (Dermatology), Vanderbilt University, Nashville, Tennessee.
Biochem Biophys Res Commun. 1988 May 31;153(1):183-90. doi: 10.1016/s0006-291x(88)81206-3.
Different tyrosines are autophosphorylated on the native and on the protease-generated 150 kDa forms of the epidermal growth factor receptor. High ATP concentrations increase the apparent molecular weight of already phosphorylated native receptors but not of the 150 kDa form, indicating that only the native receptor has multiple autophosphorylation sites available. The non-identity of the tyrosine-phosphates on the native and 150 kDa receptor forms is seen in their response to alkaline hydrolysis (10% and 40% resistant, respectively). Since the liberated phosphate is peptide bound, the native receptor fails to be alkali-resistant because of which peptide bonds are hydrolyzed.
在天然的和蛋白酶产生的150 kDa形式的表皮生长因子受体上，不同的酪氨酸会发生自身磷酸化。高ATP浓度会增加已磷酸化的天然受体的表观分子量，但不会增加150 kDa形式的受体的表观分子量，这表明只有天然受体具有多个可用于自身磷酸化的位点。天然受体和150 kDa受体形式上的磷酸酪氨酸在对碱性水解的反应中表现出不同（分别为10%和40%抗性）。由于释放的磷酸盐与肽结合，天然受体不能抗碱，因为其肽键会被水解。
