F1‐ATPase from Micrococcus sp. ATCC 398

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Abstract
The preparation of highly purified F1‐ATPase from Micrococcus sp. ATCC 398 by application of DEAE‐Sepharose CL‐6B chromatography as final step is described. This enzyme consists of five subunits of different molecular weight: α (65000), β (55000), γ (35000), δ (20000), and ∈ (17000). Disc electrophoresis on 5% polyacrylamide gels removes the ∈‐polypeptide yielding an active ATPase complex with four different subunits: α, β, γ, δ. Additionally, by variation of the ionic strength δ can be (partly) removed allowing the isolation by disc electrophoresis of an active ATPase complex which consists only of three different subunits α, β, and γ. If the DEAE‐Sepharose chromatography is carried out in the absence of diisopropyl phosphofluoridate (auto)proteolysis yields both an active ATPase with the subunits α+ (mol. wt 61000), β, γ, and δ and an inactive protein complex with the subunits α+, β, γ, δ, and two additional polypeptides a (mol. wt 38000) and b (mol. wt 23000). The latter two polypeptides are supposedly fragments of α+‐chains which have become partially cleaved by (auto)proteolysis.

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