Abstract
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 |
|---|---|
| Original language | Russian |
| Pages (from-to) | 1100-1108 |
| Number of pages | 9 |
| Journal | Biokhimiya |
| Volume | 57 |
| Issue number | 7 |
| State | Published - Jul 1992 |