Yoshida M, Poser J W, Allison W S, Esch F S
J Biol Chem. 1981 Jan 10;256(1):148-53.
The TF1-ATPase from the thermophilic bacterium, PS3, is inactivated by dicyclohexylcarbodiimide (DCCD). This inactivation is stimulated by ADP and other specific nucleotides and is inhibited by Mg2+. When the inactivation is carried out with [14C]DCCD, about 2 g atoms of 14C are bound/mol of TF1 when the enzyme is nearly completely inactivated. The isolated subunits from TF1 inactivated with [14C]DCCD contain the following amounts of 14C/mol: alpha, 0.12 g atom; beta, 0.47 g atom; gamma, approximately 0.04 g atom; delta, none; and epsilon, 0.05 g atom. Fractionation of tryptic digests have shown that the 14C bound to the alpha subunit is nonspecifically associated with several peptides, and that the 14C bound to the beta subunit is associated with a single tryptic peptide with the amino acid sequence Ala-Gly-Val-Gly-Glu-Arg, where Glu represents the N-gamma-glutamyl derivative of dicyclohexyl[14C]urea.
来自嗜热细菌PS3的TF1 - ATP酶被二环己基碳二亚胺（DCCD）灭活。这种灭活作用受到ADP和其他特定核苷酸的刺激，并被Mg2 +抑制。当用[14C]DCCD进行灭活时，当酶几乎完全失活时，每摩尔TF1结合约2克原子的14C。用[14C]DCCD灭活的TF1分离出的亚基每摩尔含有以下量的14C：α亚基为0.12克原子；β亚基为0.47克原子；γ亚基约为0.04克原子；δ亚基没有；ε亚基为0.05克原子。胰蛋白酶消化产物的分级分离表明，与α亚基结合的14C与几种肽非特异性相关，而与β亚基结合的14C与一种胰蛋白酶肽相关，其氨基酸序列为Ala - Gly - Val - Gly - Glu - Arg，其中Glu代表二环己基[14C]脲的N - γ - 谷氨酰衍生物。
