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[Biochemical modifications in a case of analbuminemia (author's transl)].

J P Goulle·G Laine·F Sauger·B Maitrot·A Bouillerot·H Gray·P Blondet·B Dieryck
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Abstract

A new case of analbuminemia is described for a six month old child of Algerian origin. The serum albumin concentration was 64 mg/l and its immunochemical action was identical to that of normal albumin. The system reacted by an increase of the synthesis of globulins. For the subject, the alpha1-antitrypsin, ceruloplasmin, haptoglobin, alpha2-macroglobulin, transferrin and immunoglobulins M contents were three times higher than the standard figures. However, it was possible to show that the presence of free bilirubin independent from proteins could be detected at a concentration of 17 mumol/l.

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BilirubinCeruloplasminHaptoglobinsHumansImmunoglobulin MInfantSerum AlbuminSerum GlobulinsTransferrinalpha-MacroglobulinsCase ReportsComparative StudyEnglish AbstractJournal Article

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J P Goulle, G Laine, F Sauger, B Maitrot, A Bouillerot, H Gray, P Blondet, B Dieryck. 1976-09-06. [Biochemical modifications in a case of analbuminemia (author's transl)].. https://doi.org/10.1016/0009-8981(76)90524-6

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PubMed1979

Human alpha-fetoprotein. Fluorescence studies on binding and proximity relationships for fatty acids and bilirubin.

The binding of bilirubin and the polyene fatty acids cis-parinaric acid and cis-eleostearic acid to human alpha-fetoprotein was studied using fluorescence quenching and fluorescence enhancement techniques. alpha-Fetoprotein has three fatty acid binding sites of decreasing affinity (association constants 2.1 x 10(7) M-1 9.1 X 10(5) M-1, and 1.4 x 10(5) M-1) and one relatively strong and one relatively weak bilirubin binding site (association constants 1.1 x 10(7) M-1 and 1.8 x 10(5) M-1). These association constants are slightly weaker than the corresponding association constants for binding to human albumin. Competition experiments failed to show preferential binding of polyunsaturated fatty acids. Fluorescence quenching was used to determine 11 ligand-ligand and ligand-tryptophanyl residue distances. Each of these 11 calculated distances (ranging from 19 A to 32 A) was within 5 A of the corresponding distances measured previously for human albumin (Berde, C.B., Hudson, B.S., Simoni, R.D., and Sklar, L.A. 1979, J. Biol. Chem. 254, 391-400). Thus, in addition to previously described sequence homology, immunologic cross-reactivity, and other similarities, human albumin and human alpha-fetoprotein have functional and geometric homologies.

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