| Abstract: | Determination of the amino acid composition of coelomic hemerythrin from Golfingia gouldii shows 3 arginine residues and 10 to 11 lysine residues per protein subunit of 13,500 molecular weight. On this basis, the 28 to 30 major peptide spots revealed by electrophoresis and chromatography of tryptic hydrolysates would indicate two kinds of subunit. However, similar evidence from chymotryptic hydrolyses is not unequivocal, since the number of peptide spots is also compatible with an assumption of only one kind of chain. In addition to indicating the possible existence of two types of subunit, the peptide maps of enzymic digests of hemerythrin from individual animals shows at least one and perhaps more differences in peptide composition. |
