嗜热细菌PS3的F1 - ATP酶在65摄氏度下被5'-对氟磺酰苯甲酰肌苷灭活的同时，β-酪氨酸-364也发生了修饰。
Inactivation of the F1-ATPase from the thermophilic bacterium PS3 by 5'-p-fluorosulfonylbenzoylinosine at 65 degrees C is accompanied by modification of beta-tyrosine-364.
作者信息
Bullough D A, Allison W S
机构信息
Department of Chemistry, University of California, San Diego, La Jolla 92093.
出版信息
Biochim Biophys Acta. 1988 Jul 27;934(3):397-400. doi: 10.1016/0005-2728(88)90097-7.
A major radioactive peptide, T1, was resolved by high-performance liquid chromatography from a tryptic digest prepared from the F1-ATPase from the thermophilic bacterium PS3 which had been inactivated with p-fluorosulfonylbenzoyl[3H]inosine. Two radioactive peptides, T1P1 and T1P2, were isolated from a peptic digest of T1 by high-performance liquid chromatography. The sequences of T1P1 and T1P2 were shown to be E-E-H-X-Q-V-A-R and E-E-H-X-Q, respectively, where X corresponds to derivatized Tyr-364 of the beta subunit.
一种主要的放射性肽T1，通过高效液相色谱法从嗜热细菌PS3的F1-ATP酶经对氟磺酰苯甲酰[3H]肌苷失活后制备的胰蛋白酶消化物中分离出来。通过高效液相色谱法从T1的胃蛋白酶消化物中分离出两种放射性肽T1P1和T1P2。结果表明，T1P1和T1P2的序列分别为E-E-H-X-Q-V-A-R和E-E-H-X-Q，其中X对应于β亚基的衍生化酪氨酸-364。
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