| pubmed-article:12412500 | pubmed:abstractText | A multi-step purification procedure has been used for isolation of alpha 2M/LRP receptor from human placenta. Enzymatic properties of complexes of purified alpha 2M trypsin with alpha 2M/LRP receptor were studied. This complex is characterized by enzymatic activity measured by a kinetic procedure based on the trypsin reaction with synthetic substrate alpha 2N-benzoyl-D,L-arginine nitroparaanilide. Purified triple complexes of alpha 2M trypsin with alpha 2M/LRP had 22-28% residual trypsin activity, while that of trypsin complex with alpha 2-macroglobulin was 52-53%. Patients' blood samples were characterized by a high level of residual activity of the studied double and triple complexes only initially. A decrease in the activities of these complexes was observed in patients with high levels of malonic dialdehyde (by TBA-reactive products) combined with decreased level of superoxidedismutase-like activity. | lld:pubmed |
