Acid phosphatase isoenzymes of Chlamydomonas reinhardii
作者： Anna H. Nagy , Géza Erdös , Natalia N. Beliaeva , István Gyurján
DOI: 10.1007/BF00272924
关键词:
摘要: Acid phosphatase isoenzymes of Chlamydomonas reinhardii were investigated by isoelectric focusing in polyacrylamide gel systems. In this paper we describe detail an original method for acid phosphatases extracted from wild-type and phosphatase-lacking mutant algae, obtained Laboratoire de Genetique University Liege. Three can be separated the buffer-soluble components these cells. An additional isoenzyme type visualized using nonionic detergent NP40 as solubilizer. We conclude that four are related to structural gene soluble constitutive phosphatase, which was shown their appearance P2 total absence Pa. The pI values range between pH 5.2 6.2. As a result treatment with extracts both lines contain two active forms characterized high heat resistance low values. These enzymes fully either alpha-naphthyl phosphate or different acetate esters substrates.
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