FRACTIONATION AND PARTIAL CHARACTERIZATION OF PROTEINS EXTRACTED FROMTHE BOVINE FALLOPIAN-TUBE - PREPARATION OF REAGENTS FOR FURTHER PURIFICATIONS

Described in the present paper is a combined biochemical and immunolog ical approach to study oviductal proteins in the bovine. Antisera were raised against semi-purified proteins extracted from bovine tubal muc osal tissue and were characterized. These antisera are available to mo nitor purifications of specific oviductal: proteins in the future. Ovi ducts from 170 cyclic cows were collected at a slaughterhouse, and hig h amounts of mucosal proteins were extracted. The proteins were fracti onated after precipitation with ammonium sulfate, anti-bovine serum al bumin (bSA) and anti-bovine immunoglobulins (bIg) affinity chromatogra phy and ion exchange chromatography. Each of the 12 fractions obtained after ion exchange chromatography was used to immunize a rabbit. Cond itioned media were recovered from bovine oviduct cell monolayers cultu red without serum to confirm the oviductal origin of the extracted pro teins. After Western blot analysis, 15 proteins were detected in the b ovine oviductal extracts, and their molecular weights and isoelectric points were determined by 2 dimensional electrophoresis. Among these 1 5 proteins, II were also detected in conditioned media of bovine ovidu ctal cells. These results demonstrate an oviductal origin of the II de tected proteins and strongly suggest their secretion by the oviductal cells.