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- W2109992783 abstract "Mammalian spermatozoa are particularly susceptible to the deleterious effects of reactive oxygen species and lipid peroxidation, which ultimately lead to impaired fertility. A number of enzymes are present in the male reproductive tract which may play a role in preventing oxidative damage; in particular, the epididymis is the site of synthesis and secretion of large amounts of extracellular superoxide dismutase (eSOD). In order to study the distribution of eSOD in the male reproductive tract, and distinguish it from other related superoxide dismutase isoenzymes (e.g. cytosolic SOD), polyclonal antisera have been raised against a recombinant human eSOD fusion protein, expressed in bacterial cells. This protein was expressed from a synthetic gene fragment, using preferred Escherichia coli codons, designed to overcome the problems associated with the high guanine+cytosine content of the natural human eSOD transcript. Using this antiserum, eSOD can be readily detected in a range of human reproductive tissues as well as in human seminal plasma. However, the presence of similar levels of eSOD in the seminal plasma of vasectomized men (probably of prostatic origin) precludes its use as a simple diagnostic indicator of eSOD activity levels in the epididymis." @default.
- W2109992783 created "2016-06-24" @default.
- W2109992783 creator A5011618079 @default.
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- W2109992783 date "1998-03-01" @default.
- W2109992783 modified "2023-10-18" @default.
- W2109992783 title "Expression of extracellular superoxide dismutase in the human male reproductive tract, detected using antisera raised against a recombinant protein" @default.
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- W2109992783 doi "https://doi.org/10.1093/molehr/4.3.235" @default.
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