1. Diamine oxidase [amine-oxygen oxidoreductase (deaminating)(pyridoxal-containing), EC 188.8.131.52] was purified from human seminal plasma more than 1,700-fold. The enzyme appeared to be homogeneous on polyacrylamide-gel electrophoresis at two different pH values. 2. The general properties of the enzyme were comparable with those described for other diamine oxidases from different mammalian sources. The molecular weight of the enzyme was calculated to be about 182,000. 3. The enzyme had highest affinity for diamines, but polyamines spermidine and spermine were also degraded at concentrations that can be considered physiological in human semen. 3. The possible degradation of spermine by diamine oxidase in human semen in vivo may give rise to the formation of cytotoxic aldehydes that conceivably can influence the motility and survival of the spermatozoa.
Research Article| February 01 1975
Oxidation of polymines by diamine oxidase from human seminal plasma
Biochem J (1975) 145 (2): 373-378.
- Views Icon Views
- Share Icon Share
- Cite Icon Cite
E Hölttä, P Pulkkinen, K Elfving, J Jänne; Oxidation of polymines by diamine oxidase from human seminal plasma. Biochem J 1 February 1975; 145 (2): 373–378. doi: https://doi.org/10.1042/bj1450373
Download citation file: