Changes in the surface of mouse spermatozoa during their passage through the epididymis
نویسنده
چکیده
components, chymosins I and 11, by column chromatography on DEAE-cellulose (Fig. 1). The same characteristic profile was obtained from four different animals. Pooled fractions of chymosins I and I1 were examined by urea/polyacrylamide-gel electrophoresis, and each consisted of one major protein species, with chymosin I1 showing a slightly higher electrophoretic mobility than chymosin I. Chymosins I and I1 were not distinguishable by electrophoresis in sodium dodecyl sulphate/polyacrylamide gels. The chromatographic profile of individual calf chymosin contrasted with that of commercial crystalline chymosin, which showed a more complex profile similar to that described by Foltmann (1966) and consisting of fractions designated chymosins A, B and C by that author. Prochymosin from an individual stomach was not resolved into two distinct fractions by DEAE-cellulose chromatography, but was eluted as a single skewed peak. However, urea/polyacrylamide-gel electrophoresis of the chromatographic product clearly showed the presence of two major protein components with slightly different electrophoretic mobilities. Further characterization of chymosins I and I1 was carried out by electrophoretic comparison in urea/polyacrylamide gels with authentic specimens of chymosins A and B obtained from crystalline chymosin by DEAE-cellulose chromatography. Three of the four stomachs utilized in the study were examined in this way. In all cases chymosin I1 showed the same mobility as chymosin B, whereas chymosin I was distinct from both chymosins A and B. It is likely therefore that chymosin I1 and chymosin B are identical. Presumably an extension of these studies would reveal stomachs containing the A variant. Further preliminary experiments indicate that chymosin I is not an artifact of the extraction/activation procedure. The possibility that chymosins I and 11 represent separate non-allelic genes cannot be discounted. Alternatively they may be related as a result of post-translational modification of a single polypeptide.
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Assessment of Sialic Acid Distribution in Mouse Epididymis
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