Abstract
IN the transformation of ovalbumin to plakalbumin by a proteinase from Bacillus subtilis, a small amount of material containing non-protein nitrogen is released, which has been separated into three fractions, designated1 A, B, and C. Amino-acid analysis of these fractions suggests that A and B are peptides composed chiefly of glycine, valine, aspartic acid and alanine, in the ratios 1 : 1 : 1 : 3 and 1 : 1 : 1 : 1, respectively, while C appears to be alanylalanine. As pointed out before1, it is reasonable to suppose that the three peptide fractions arise all from the same segment of the ovalbumin molecule, represented by A. Accordingly, B and C should be identical with parts of A. The present investigation furnishes some evidence for this scheme.
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