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Analogues in other mammals and in fish of human plasma proteins, C-reactive protein and amyloid P component

Abstract

TWO apparently disparate human plasma proteins, C-reactive protein (CRP) and amyloid P component (protein SAP)1, have been shown to have substantial homology of amino acid sequence, similar subunit composition and similar molecular appearance in the electron microscope2. We now report for the first time the isolation (using calcium-dependent affinity chromatography) of proteins closely resembling human SAP, from sera of other mammals, amphibia and fish, and of proteins from the plaice (Pleuronectes platessa L.) and the chicken, which closely resemble human CRP. The stable evolutionary conservation in this plasma protein family of calcium-dependent ligand-binding specificity and molecular architecture during much of vertebrate evolution implies that they have important functions, and also facilitates their experimental investigation.

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