Primary Structure of Lysozymes from Man and Goose

The primary structure of goose egg white lysozyme seems to be distinct from that of hen egg white and human leukaemia lysozymes.     

Microheterogeneity of cross-linked gamma dimers isolated from bovine stabilized fibrin

Bovine stabilized fibrin was reduced, carboxymethylated and separated by chromatography on a Sepharose 4B column. The fraction containing cross-linked γ dimers was then subjected to linear gradient chromatography on a CM-52 column. On this column, the γ dimers were separated into an adsorbed and unadsorbed fraction. The components in these fractions were designated as the γ-1 and γ-2 dimers. They each gave a single band on SDS-polyacrylamide gel electrophoresis and both had a molecular weight of 90,000 (±2,000). The identities of the γ-1 and γ-2 dimers were also shown by their amino acid compositions, terminal residues and tryptic and plasmic maps. However, they differed in electrophoretic mobilities on gels at pH 8.3 and pH 3.6 and in carbohydrate composition. The γ-1 dimer was slightly acidic and contained more hexoses and glucosamine than the γ-2 dimer. These results indicate that the characteristics of the bovine monomeric γ chains, γ-1 and γ-2, previously reported by Gerbeck $\text{et al}$., are transferred to their corresponding cross-linked γ dimers, formed in the stabilization of fibrin.