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- W2000558603 abstract "Major basic protein (MBP)‡ was measured by radioimmunoassay (RIA) using 131I-MBP, rabbit anti-MBP, and burro anti-rabbit IgG. Two critical features of the assay were: (1) alkylation of the MBP with iodoacetamide prior to radioiodination and (2) inclusion of another basic protein, either protamine or histone, in the phosphate buffer. Freshly isolated non-alkylated MBP was immunologically deficient when compared to alkylated or reduced and alkylated MBP, but its reactivity could be restored by reduction with dithiothreitol and alkylation. Polymerized MBP also showed reduced immunoreactivity which could be regenerated by reduction and alkylation. MBP activity was rapidly destroyed at 56°C, but it could be lyophilized, and it survived treatment with 6 M guanidinium hydrochloride (GuHCl). After initial reduction and alkylation in the absence of dissociating solvents, subsequent reduction and alkylation in 6 M GuHCl renders the protein unreactive. MBP levels in normal guinea pig serum were less than 5 ng/ml and were not elevated in sera from guinea pigs parasitized with Trichiwlla spiralis and having peripheral blood eosinophilia. Muscle extracts from Trichinella infected animals showed significantly higher levels of MBP activity than normal controls. MBP was measurable in extracts of untreated eosinophils, but reduction and alkylation of these extracts increased MBP activity several fold. Extracts of purified eosinophils averaged 1.13 × 10−3 ng MBP per cell. The RIA permits detection of MBP in body fluids and tissues at levels as low as 2 ng/ml. The RIA is useful in assessing increased or decreased levels of MBP activity in samples from experimental animals when compared to samples from controls." @default.
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- W2000558603 date "1979-09-01" @default.
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- W2000558603 title "Measurement of guinea pig eosinophil major basic protein by radioimmunoassay" @default.
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- W2000558603 doi "https://doi.org/10.1016/0161-5890(79)90012-9" @default.
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