Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-11-4
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.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0869-2084
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7-11
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
[Properties and expression of the human activated alpha2-macroglobulin receptor].
pubmed:publicationType
Journal Article, English Abstract