1921
Volume 50, Issue 2
  • ISSN: 0002-9637
  • E-ISSN: 1476-1645
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Abstract

Abstract

The salivary gland activities of apyrase, an enzyme that prevents platelet aggregation by eliminating ADP, were compared among five members of the species complex and . Within the group, exhibited the lowest amount of enzyme activity at all pH levels measured. Apyrase activity could be separated into three groups at pH 7.5 and 8.0. The two most anthropophilic species ( and ) exhibited higher activity at pH 9.0. and , both saltwater taxa, and , a New World species, exhibited peak apyrase activity at pH 8.0. When the effects of divalent cations (Ca++, Mg++) on enzyme activity were compared at pH 8.5, apyrase activity in the presence of Mg++ could be separated into three levels. and exhibited reduced activity in the presence of Mg++. , and displayed the highest relative levels of activity. , with a Mg:Ca ratio of 0.80, was most similar to . These biochemical differences suggest that different isoenzymes of apyrase have developed within the genus .

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/content/journals/10.4269/ajtmh.1994.50.235
1994-02-01
2017-11-20
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