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[40] H+-ATPase from plasma membranes of Saccharomyces cerevisiae and Avena sativa roots: Purification and reconstitution

1988; Academic Press; Linguagem: Inglês

10.1016/0076-6879(88)57102-1

1557-7988

Ramón Serrano,

Lipid metabolism and biosynthesis

This chapter focuses on the purification and reconstitution of H+-ATPase from plasma membranes of Saccharomyces cerevisiae and arena sativa roots. The plasma membranes of fungi and plants contain a similar ATPase, which represents a novel type of proton pump. Two convenient sources for these enzymes are bakers' yeast (Saccharomyces cerevisiae) and oat (Arena sativa) roots. The purified plasma membrane ATPases from these organisms can be reconstituted into proteoliposomes that catalyze ATPdriven proton transport. A summary of the purification of the yeast and oat root plasma membrane ATPases is shown in the chapter. The evaluation of the purifications is complicated by the activating and inactivating effects of detergents. Detergent activation results from unmasking latent enzyme molecules present in closed vesicles, while detergent inactivation may be caused by delipidation of the enzymes. The purified plasma membrane ATPase from yeast and oat roots contain a major polypeptide of about 105 kDa, which represents more than 70–80% of the protein in the preparations. Some minor polypeptides of lower molecular weight are usually present in variable and less than stoichiometric amounts.