Date of Award:
5-1-1977
Document Type:
Thesis
Degree Name:
Master of Science (MS)
Department:
Biology
Department name when degree awarded
Life Sciences:Biology
Committee Chair(s)
LeGrande C. Ellis
Committee
LeGrande C. Ellis
Abstract
Preparations of mature rat testes were assayed for phospholipase A2 activity. Two separate phospholipase A2 enzymes were observed with two pH optima: one at pH 3.5 and the second at pH 7.5-8.0. Further investigation suggested that the acidic phospholipase A2 was associated with the interior of the lysosomes (i.e., was a soluble enzyme) whereas the alkaline phospholipase A2 was associated with the lysosomal and plasma membranes. Acid optimal pH phospholipase A2 activity was observed primarily in the lysosomes and germinal elements that were ' manually extruded from the seminiferous tubules. Some alkaline pH optimal phospholipase A2 activity was localized in the interstitial cells, but the bulk occurred in the seminiferous tubules. The bulk ) of the seminiferous tubular activity was observed in the extruded germinal cells. Considerable amounts of alkaline pH optimal phospholipase A2 were observed in the teasing media and the media where the germinal elements were extruded from the seminiferous tubules, indicating that it was easily displaced from the plasma membranes.
Recommended Citation
Boccio, James R., "The Localization and Partial Characterization of Rat Testicular Phospholipase A2" (1977). Biology. 419.
https://digitalcommons.usu.edu/etd_biology/419
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