The structural organization of extracellular repressible acid phosphatase from S. cerevisiae has been studied. The existence of multiple acid phosphatase forms with isoelectric points at pH 4.1-4.8 has been confirmed by isoelectrofocusing. The molecular masses of three acid phosphatase isoforms (56, 57-59, and 60 kDa) obtained after enzymatic deglycosylation correlate with the data obtained previously during the analysis of translation products in cell-free systems. Electron microscopic studies revealed that the acid phosphatase molecule has a square shape and is made up of four identical subunits with molecular masses of about 125 kDa.
|Translated title of the contribution||Analysis of the quaternary structure of secreted repressible acid phosphatase from the yeast Saccharomyces cerevisiae|
|Number of pages||9|
|State||Published - Jul 1 1992|