Preparation of Fragments 505-582 and 505-573 of Bovine Serum Albumin

Abstract

Peptic fragment 505-582 of bovine serum albumin, the "Phe" fragment, has been found useful in several laboratories for studies of antigenic sites, ligand binding and metabolism. It contains the entire carboxyterminal loop, Loop 9, of the albumin molecule. We present an improved preparation of this peptide. Peptide 505-582 is obtained in about 9% yield, along with a similar yield of the closely associated peptide 505-573 arising from a second peptic cleavage. The unusual ultraviolet absorption spectrum of these peptides shows triple maxima near 259 nm reflective of the high phenylalanine content and the total absence of tyrosine and tryptophan.