[Analysis of the quaternary structure of secreted repressible acid phosphatase from the yeast Saccharomyces cerevisiae].
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.
Shnyreva
M G
MG
Tsuprun
V L
VL
Stel'mashchuk
V Ia
VIa
Egorov
S N
SN
D000135:Acid Phosphatase / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D008854:Microscopy, Electron; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D000135:Acid Phosphatase