Analysis of the quaternary structure of secreted repressible acid phosphatase from the yeast Saccharomyces cerevisiae
Shnyreva, M.G.; Tsuprun, V.L.; Stel'mashchuk, V.I.; Egorov, S.N.
Biokhimiia 57(7): 1100-1108
1992
ISSN/ISBN: 0320-9725 PMID: 1391215 Document Number: 398037
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.