Some immunochemical properties of pollen extracellular nuclease

The extracellular nuclease fromPinus silvestris pollen was isolated and characterized. Molecular sieving produced only one peak of nuclease with apparent molecular mass of about 30 kDaltons, while molecular mass of the enzyme as determined by means of sodium dodecyl sulphate-DNA gel electrophoresis was 25.7 kDaltons or less. The nuclease exhibited one electrophoretic molecular form only. Specific antiserum against this nuclease was prepared and the nuclease was shown to be immunochemically cross-reactive with extracellular nuclease from Pinus nigra pollen. No immunochemical relationships were observed between pine nuclease and the pollen extracellular nucleases from the angiosperm species,Nicotiana tabacum, Corylus avellana, Alnus incana andBetula pubescens. No cross-reactivity was detected by double diffusion between the pine nuclease and the extracellular proteins from vegetative spores ofEquisetum arvense.