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By V.M. Rosenoer

ISBN-10: 0080196039

ISBN-13: 9780080196039

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1974) Non-specific binding of proteins by substituted agaroses. In: Immobilized Biochemicals and Affinity Chromatography. R. B. Dunlap, editor, pp. 43-59. Plenum Publ. Y. 123b. Hofstee, B. H. J. (1975) Fractionation of protein mixtures through differential adsorption on a gradient of substituted agaroses of increasing hydrophobicity. Prep. Biochem. 5, 7-19. 124. Memoli, V. A. and G. J. Doellgast (1975) Hemoglobin and serum albumin: salt-mediated hydrophobic chromatography. Biochem. Biophys. Res.

The helices should start at the Cys residues and wind antiparallel for about six turns or 20 residues. These helical rods would be about 32 Ä long and with some additional length for the hairpin turns at each end, the structure would fit well the short axis of albumin of about 40 Ä. (46) Although a Pro residue will accommodate the geometry of the alpha-helix, the absence of a hydrogen bond on its nitrogen atom weakens a helix, so that the relative absence of Pro in the twelve proposed helical sections supports the model.

132. Craig, L. C , H. C. Chen and E. J. Harfenist (1969) Separation based on size and conformation. In: Progress in Separation and Purification, T. Gerritsen, editor, pp. 219-238. Wiley, New York. 133. Van Oss, C. J. (1970) Ultrafiltration membranes. In: Progress in Separation and Purification, E. S. Perry, editor, pp. 97-132. Wiley, New York. 134. Pedersen, K. O. (1962) Exclusion chromatography. Arch. Biochem. , suppl. 1, 157-168. 135. Pedersen, K. O. and L. O. Andersson (1963) Fractionation of serum albumin on sephadex.

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Albumin: Structure, Function and Uses by V.M. Rosenoer

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