Extracellular folate deaminase of Dictyostelium discoideum

Folate deaminase released from cells of Dictyostelium discoideum is heterogenous with respect to molecular weight and stability at 60°C. The most heat-stable component isoelectrofocuses in a broad band at approx. pH 6. The K m value of this component for folate is approx. 7 · 10 −7 M and M r approx....

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Published inBiochimica et biophysica acta Vol. 677; no. 2; pp. 295 - 302
Main Authors Bernstein, R.L., Tabler, M., Vestweber, D., Van Driel, R.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 12.10.1981
Subjects
Aminohydrolases - metabolism
Cyclic AMP - metabolism
D. discoideum
Dictyostelium - metabolism
Extracellular enzyme
Folate deaminase
Folic Acid - metabolism
fungi
Hot Temperature
Hydrogen-Ion Concentration
Molecular Weight
Protozoan Proteins
D. discoideum
Folate deaminase
Extracellular enzyme
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Summary:Folate deaminase released from cells of Dictyostelium discoideum is heterogenous with respect to molecular weight and stability at 60°C. The most heat-stable component isoelectrofocuses in a broad band at approx. pH 6. The K m value of this component for folate is approx. 7 · 10 −7 M and M r 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.
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ISSN:0304-4165
0006-3002
1872-8006
1878-2434
DOI:10.1016/0304-4165(81)90099-4