Biomedical subjects
K Elfving
Publications and source records attributed to K Elfving.
Oxidation of polymines by diamine oxidase from human seminal plasma.
1. Diamine oxidase [amine-oxygen oxidoreductase (deaminating)(pyridoxal-containing), EC 1.4.3.6] 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.
Association of spermine and diamine oxidase activity with human spermatozoa.
Human spermatozoa, separated from the seminal plasma, contained substantial amounts of spermine, and also a distinct diamine oxidase (EC1.4.3.6) activity. Spermine, but not diamine oxidase activity, could be removed from the spermatozoa by washing the cells with buffers containing high concentrations of salts. Incubation of human spermatozoa in the presence of labelled spermine and partly purified amine oxidase from bovine blood gave rise to the formation of radio-active products that could not be removed from the spermatozoa by increasing the ionic strength. Similarly, partly purified diamine oxidase from human seminal plasma apparently catalysed the formation of labelled products from radioactive spermine that were more tightly bound to the spermatozoa than spermine itself.