[Properties and expression of the human activated alpha2-macroglobulin receptor].
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.
Zhloba
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AA
Ivanova
S Iu
SIu
D001161:Arteriosclerosis / Q000097:blood / Q000188:drug therapy; D005260:Female; D006801:Humans; D026503:Low Density Lipoprotein Receptor-Related Protein-1 / Q000097:blood* / Q000302:isolation & purification; D008875:Middle Aged; D009000:Monocytes / Q000378:metabolism; D010920:Placenta / Q000737:chemistry; D014357:Trypsin / Q000097:blood; D000511:alpha-Macroglobulins / Q000378:metabolism
D026503:Low Density Lipoprotein Receptor-Related Protein-1; D000511:alpha-Macroglobulins; D014357:Trypsin