Biotinylated-Enzymes Affinity Cytochemistry to Demonstrate Endogenous Avidin in Hen Oviducts-Preliminary Study
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Biotinylated-enzymes affinity cytochemistry using biotinyl-horseradish peroxidase (B-HRP) and -alkaline phosphatase (B-ALPase) was investigated in the laying hen oviduct. Endogenous biotin-binding activities (EBBA) were demonstrated in granules of tubular gland cells and non-ciliated unicellular epithelial cells in both the lower magnum and the isthmus when the ovum descended into the lower isthmus or uterus. Biotin affinity secretory granules were electron dense and inhomogenous (or cored with dense and less dense regions) and the in size varied from large to small in acinar cells and to small in the epithelium, respectively.<BR>Utilizing this method, EBBA suppressed oviductal tissue synthesizing endogenous avidin, thus facilitating the interpretation of a specific avidin-biotin reaction system introduced into the various histo- and cytochemical tools.<BR>On the other hand, the resultant demonstration of avidin disagrees with ordinal data that had beeh localized in the oviductal goblet cells obtained from chicken oviduct stimulated by ovarian hormones. It is desirable to study the localization of immunoreacting and B-HRP and/or B-ALPase affinity avidin using ovulation occurring in a 24 hr daily period in hens or quails, and/or non-laying ones given gonadal hormones.
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