Extracellular folate deaminase of Dictyostelium discoideum
| Autor: | R.L. Bernstein, R. Van Driel, M. Tabler, D. Vestweber |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Hot Temperature
Protozoan Proteins Biophysics Biochemistry Dictyostelium discoideum Folic Acid Aminohydrolases Cyclic AMP Extracellular Lentil lectin Dictyostelium Molecular Biology chemistry.chemical_classification biology food and beverages Broad band Hydrogen-Ion Concentration biology.organism_classification Molecular biology Molecular Weight Enzyme chemistry Concanavalin A biology.protein Glycoprotein |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - General Subjects. 677:295-302 |
| ISSN: | 0304-4165 |
| DOI: | 10.1016/0304-4165(81)90099-4 |
| Popis: | Folate deaminase released from cells of Dictyostelium discoideum is heterogeneous with respect to molecular weight and stability at 60 degrees C. The most heat-stable component isoelectrofocuses in a broad band at approx. pH 6. The Km value of this component for folate is approx. 7 x 10(-7)M and Mr approx. 40 000. The major portion if not all of the deaminase binds to immobilized concanavalin A and lentil lectin. Extracellular folate deaminase has a pH-optimum of approx. pH 6.0. This is higher than that of lysosomal enzymes, which are also glycoproteins released into the extracellular medium. |
| Databáze: | OpenAIRE |
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