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Biology of Reproduction, Vol 14, 233-245, Copyright © 1976 by Society for the Study of Reproduction
1 Department of Environmental Studies,
Trinity University,
San Antonio, Texas 78284 Ovarian follicles contain at least two "collagenolytic" enzymes that can be detected by an assay
in which follicular tissue is cultured on gels composed of reconstituted collagen. One enzyme is
most active at pH 5.5 (with a range of 4.0-6.8), and is detectable within 10-15 h after tissue
incubation. The other enzyme is active at physiological pH (7.0-7.8), but requires approximately
30 h of incubation before the collagen gels begin to exhibit digestion. Both enzymes are present in
appreciable amounts in mature Graafian follicles. They are inhibited by EDTA, alpha2-macroglobulin, fetal calf serum, rabbit serum, and high concentrations of ascorbic acid. Chloroquine
inhibits the activity at pH 7.4, but does not affect the enzyme that is active at pH 5.5. Neither
enzyme is distinctly inhibited by cysteine, trypsin inhibitor (Kunitz), ceruloplasmin, indomethacin,
or alpha1-antitrypsin. In consideration of various ovarian factors which may influence the
expression of this collagenolytic activity, it is concluded that these enzymes could be active in the
digestion of the follicle wall during ovulation.
Note:
ACKNOWLEDGMENTS
We are thankful to Dr. Andrew G. Cowles for his
generous donation of the electron microscope and
other facilities essential to the conduct of this study.
This research was supported by NIH Grant HD-06371.
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