Open AccessSeveral compartments of Saccharomyces cerevisiae are equipped with Ca 2+ ‐ATPase(s)
Author(s) -
Okorokov Lev A.
Publication year - 1994
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1994.tb06785.x
Subject(s) - endoplasmic reticulum , golgi apparatus , membrane , yeast , atpase , biochemistry , saccharomyces cerevisiae , cellular compartment , concanavalin a , enzyme , microsome , phosphate , chemistry , secretory pathway , calcium atpase , cell fractionation , fractionation , biology , chromatography , cell , in vitro
Sucrose density fractionation of yeast membranes revealed two major and two minor peaks of 45 Ca 2+ transport activity which all co‐migrate with marker enzymes of the endoplasmic reticulum, Golgi and membranes associated with these compartments as well as with ATPase activity measured when all other known ATPase are inhibited. Co‐migration of 45 Ca 2+ transport and ATPase activities was also found after removal of plasma membranes by concanavalin A treatment. SDS‐PAGE at pH 6.3 shows the Ca 2+ ‐dependent formation of acyl phosphate polypeptides of about 110 and 200 kDa. It is concluded that several compartments or sub‐compartments of yeast are equipped with Ca 2+ ‐ATPase(s). It is proposed that these compartments are derived from the protein secretory apparatus of yeast.