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Abstract
1. 1. Treatment of carboxymethylated horse serum albumin with formic acid yielded two main fragments with mol. wts of 42,000 and 25,000 by splitting an Asp-Pro peptide bond. 2. 2. Sequence alignments with bovine and human serum albumin gave evidence that the Asp-Pro bond corresponds to residues 365/366 in human and 363/364 in bovine serum albumin. 3. 3. Comparative treatment of serum albumin from man, bovine, rabbit, goat and hamster gave the same cleavage products. 4. 4. All serum albumins except that from horse could be further split by cyanogen bromide.
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