Amino acid sequence of a 32‐residue region around the thiol ester site in duck ovostatin

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Abstract
To obtain the amino acid sequence at the thiol ester site in duck ovostatin for comparisons with other proteins, the native ovostatin was labeled with 14CH3NH2 at the reactive thiol ester site. The modified protein was reduced, carboxymethylated, and digested with trypsin. 14C‐labeled peptides isolated by gel filtration with Sephadex G‐50, ion‐exchange chromatography on DEAE‐cellulose and HPLC were subjected to automated sequence analysis, and the stretch of 32 amino acid residues containing the 14CH3NH2‐binding site were determined. A comparison of this sequence with the corresponding sequences in α2‐macroglobulin, and complement components C3 and C4 revealed 72, 31 and 34% homology, respectively. The results indicate that ovostatin is a close relative to plasma α‐macroglobulins and may share a common ancestor with C3 and C4.