Characteristics of spermidine oxidase from sera of schizophrenic and normal subjects

ABSTRACT

Spermidine [spd] oxidase was initially purified from sera of schizophrenic and normal subjects by anion exchange chromatography. This purified the spd oxidase 105 and 128 folds, relative to the crude sera of schizophrenics and normals respectively. The specific activities of purified Spd oxidase were 231.3 and 135.2 nkat/mg protein, for schizophrenic and normal respectively. Spermidine oxidase activity was found to be linearly proportional to the amount of protein up to 900 micro g and with time of reaction up to about 50 sec. The enzyme showed a maximum activity at PH 4.5 for both schizophrenic and normal subjects. Spermidine oxidase was found to be highly activated by Ca++, ospexin and to a lesser extent, by Al+++ and folic acid. While the activity of this enzyme was found to be inhibited highly by pyrazole, antipyrine, iodoacetamide, glutathione and Inderal