
pmid: 10864517
In the process of sequencing a subtracted cDNA library from the salivary glands of the sand fly Lutzomyia longipalpis, we identified a cDNA with similarities to gene products of the adenosine deaminase family. Prompted by this cDNA finding, we detected adenosine deaminase activity at levels of 1 U/mg protein in salivary gland homogenates. The activity was significantly reduced following a blood meal indicating its apparent secretory fate. The native enzyme has a K(m) of approximately 10 microM, an isoelectric pH between 4.5 and 5.5, and an apparent molecular weight of 52 kDa by size exclusion chromatography. The possible role of this enzyme, which converts adenosine to inosine, in the feeding physiology of L. longipalpis is discussed.
DNA, Complementary, Base Sequence, Sequence Homology, Amino Acid, Adenosine Deaminase, Molecular Sequence Data, Sequence Analysis, DNA, Hydrogen-Ion Concentration, Chromatography, Gel, Animals, Amino Acid Sequence, Isoelectric Point, Psychodidae, Saliva
DNA, Complementary, Base Sequence, Sequence Homology, Amino Acid, Adenosine Deaminase, Molecular Sequence Data, Sequence Analysis, DNA, Hydrogen-Ion Concentration, Chromatography, Gel, Animals, Amino Acid Sequence, Isoelectric Point, Psychodidae, Saliva
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