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- W2034334847 abstract "Human growth hormone (GH) forms complexes with the purified proteinase inhibitor, α2-macroglobulin (α2-M). This inhibitor occurs in two different forms in serum, known as native and transformed α2-M. It has been clearly demonstrated, using chromatography and electrophoresis combined with autoradiography, that human GH binds specifically to the transformed inhibitor and not to the native protein. The binding was characterized as being mainly non-covalent and involved specific binding sites present only in the transformed inhibitor molecule. Binding analysis, using an immunoprecipitation technique, revealed that GH possesses two different types of binding sites, with dissociation constants of 0.49 ± 0.12 μmol/1 and 61 ± 8 μmol/1 for the high- and low-affinity binding site, respectively. Distribution analysis of 125I-labelled GH in whole plasma suggests that the hormone is bound to two different proteins: first, to the high-affinity GH-binding protein (GHBP) and, second, to the low-affinity GHBP, identified as transformed α2-macroglobulin." @default.
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- W2034334847 date "1996-10-01" @default.
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- W2034334847 title "Transformed α2-macroglobulin as a low-affinity growth hormone-binding protein" @default.
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- W2034334847 doi "https://doi.org/10.1111/j.1651-2227.1996.tb14315.x" @default.
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