THE COMPOSITION, STRUCTURE, AND MECHANISM OF FORMATION OF THE LINING OF THE GIZZARD OF THE CHICKEN
The extracellular protein layer which surrounds the lumen of the gizzard of the chicken has been reinvestigated to determine if it is a keratin. The lining is insoluble in keratin solvents such as urea-bisulphite or Swan's reagent as well as thioglycollate and performic acid. In addition, it contains only 1.45% sulphur so that disulphide bonds cannot play a major role in its consolidation. The lining is insoluble in acids but readily dispersed in alkali without breaking of covalent bonds. The dispersion in alkali is retarded by electrolytes. The lining is hydrolyzed by trypsin and chymotrypsin at pH 8.0 but is resistant to pepsin at pH 2.0. An alkaline dispersion of the lining is heterogeneous in the ultracentrifuge, but not grossly so, with a mean sedimentation coefficient of 5.6 svedbergs. Electron microscope studies of the lining suggest it is an amorphous, precipitated protein, which is consistent with the observation of three hazy rings in X-ray diffraction powder patterns reflecting spacings of 3.5, 4.6, and 9.4 Å. Amino acid analysis shows a ratio of more than three acidic groups to one basic, with no carbohydrate residues and little lipid in the protein layer. These observations are interpreted as indicating the precipitation of an amorphous, non-keratin, acidic, abrasion-resistant protein from the glandular mucosa by the acid in the gizzard.