Strong binding of hydrophobic anions by bovine serum albumin

SEIICHI ERA , KIYOOMI B. ITOH , MASARU SOGAMI , KAZUO KUWATA , TORU IWAMA , HIROMU YAMADA , HIROSHI W ATARI. International Journal of ...
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JONAS AND

WEBER

Strong Binding of Hydrophobic Anions by Bovine S’erum Albumin Peptides Covalently Linked to Lysozyme* Ana Jonast and Gregorio Weber

The small-peptide fraction, derived from a limited chymotryptic digestion of bovine serum albumin, and representing nearly 2 0 z of the total protein weight, contains the strong hydrophobic anion binding sites of intact albumin. When these small peptides are covalently attached t o lysozyme, used as a macromolecular support, binding of 1-anilinoABSTRACT :

I

n a previous paper (Jonas and Weber, 1970) we described the isolation, from a chymotryptic digest of BSA,’ of a heterogeneous small-peptide fraction (av mol wt