Purification and characterization of porcine heart type 2A protein phosphatases
| Autor: | Killilea Sd, Erickson Ak |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
chemistry.chemical_classification
Chromatography Ethanol Molecular mass Swine Protein subunit Myocardium Size-exclusion chromatography Phosphatase Biology Phosphate Biochemistry Isozyme chemistry.chemical_compound Enzyme chemistry Genetics Methods Phosphoprotein Phosphatases Animals Electrophoresis Polyacrylamide Gel |
| Zdroj: | Preparative biochemistry. 22(3-4) |
| ISSN: | 0032-7484 |
| Popis: | Protein phosphatases 2A1 and 2A2 were isolated from porcine heart tissue extracts by precipitation at pH 5.0 and separated by chromatography on DEAE-Sephacel. Phosphatase 2A1 was then purified to apparent homogeneity by chromatography on phenyl-Sepharose, aminohexyl-Sepharose, Sephacryl S-300, and L-tyrosine-agarose. Phosphatase 2A2 was purified to apparent homogeneity by chromatography on phenyl-Sepharose, DEAE-Sephacel, aminohexyl-Sepharose and L-tyrosine-agarose. Purified phosphatases 2A1 and 2A2 had specific activities of 2200 and 2710 nanomoles of phosphate released from phosphorylase a/mg protein, respectively. The apparent molecular weights of phosphatases 2A1 and 2A2 on gel filtration were 155 and 105 kDa, respectively. Both enzymes contain 70 and 37 kDa subunits and 2A1 also contains a 57 kDa subunit. The 37 kDa catalytic subunit (2Ac) was obtained from the purified phosphatases by treatment with room temperature ethanol followed by sucrose density gradient centrifugation or gel filtration chromatography. |
| Databáze: | OpenAIRE |
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