| Literature DB >> 6271253 |
R L Bernstein, M Tabler, D Vestweber, R Van Driel.
Abstract
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.Entities:
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Year: 1981 PMID: 6271253 DOI: 10.1016/0304-4165(81)90099-4
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002