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- W2017171480 abstract "An immunoradiometric assay and serum extraction procedure were developed to measure dimeric inhibin in porcine serum with minimal interference by putative inhibin-binding proteins. Assay sensitivity was 50 pg/tube, and it incorporated antibodies against the N-terminal region of inhibin's alpha-subunit, alpha-(1-25)-Ab, and against the C-terminal region of inhibin's beta A-subunit. To determine whether inhibin-binding proteins were present in porcine serum, serum was incubated with [125I]-recombinant human (rh)-inhibin and then chromatographed by gel filtration. Radioiodinated rh-inhibin was associated with protein(s) > 600 kDa. Radioiodinated rh-inhibin also was incubated with alpha 2-macroglobulin, an inhibin-binding protein in human and rat serum. Elution profiles were similar for serum and alpha 2-macroglobulin. Serum- and alpha 2-macroglobulin-[125I]rh-inhibin complexes dissociated upon exposure to 8 M urea. Porcine serum was treated with urea, after which inhibin was isolated and concentrated. The recovery of rh-inhibin added to starting serum was 28%. Concentrations of endogenous dimeric inhibin were < 28 pg/ml in serum collected from sows at random stages of the estrous cycle and were < 21 pg/ml in serum collected from sows 2 d postweaning. Results demonstrate that 1) concentrations of dimeric inhibin are low in porcine serum, and 2) an inhibin-binding protein(s), consistent with alpha 2-macroglobulin, is present in porcine serum." @default.
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- W2017171480 title "Measurement of dimeric inhibin in porcine serum: Evidence for low concentrations and existence of binding proteins" @default.
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- W2017171480 doi "https://doi.org/10.1016/s0739-7240(96)00086-0" @default.
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