The rationale underlying the search for evidence of genetic relatedness in the structure of homologous proteins from different species has been discussed in several previous papers (Sibley, 1960, 1962, 1964, 1965, 1967). In summary, the argument is based upon the now established facts that genetic information is encoded in the sequence of nucleotides in the genetic material, DNA, and that this sequence is translated, during the synthesis of protein molecules, into a corresponding sequence of the 20 kinds of amino acids of which proteins are composed. Thus protein molecules are genetic messages and, by a commonly accepted definition, a gene (or cistron) is the sequence of nucleotides which codes for a single polypeptide chain. A protein molecule is composed of one or more polypeptide chains. The sequence of the amino acids which are linked together by peptide bonds forms the primary structure of a polypeptide chain. In many proteins the secondary structure of the chain is the helical twist-the alpha helix-which at least some segments of the chain assume. This helical structure confers greater rigidity upon the chain. The tertiary conformation is achieved when the polypeptide chain folds upon itself in a specific fashion determined by the relationships of the side chains of the amino acids and hence by their sequence. T h e tertiary configuration is often stabilized by disulfide bridges between two cysteine residues and by non-covalent bonds of several types. Many proteins are composed of a single polypeptide chain. Others, for example hemoglobin, are composed of more than one chain. The organization of the chains of a multi-chain protein constitutes its quaternary structure. Proteins are large molecules with molecular weights usually in the range from 10,000 to 200,000 and even up to a million. For example, the egg-white proteins of the domestic fowl (Gallus gallus) include lysozyme which is a single chain of 134 amino acids with a molecular weight of 14,800 and ovalbumin which contains nearly 400 amino acid links and has a molecular weight of 45,000. Ovoconalbumin (or ovotransferrin) has a molecular weight of 76,600 and contains nearly 800 amino acids while ovomucoid has a molecular weight of 28,000 and contains about 200 amino acids. Another property of proteins is that of net charge which is the algebraic sum of the charges on the amino acids. The principal contributors to the electric charge of a protein are the ionizable groups of the side chains of lysine, arginine, glutamic acid, aspartic acid and histidine. The carboxyl and amino groups at the ends of the polypeptide chain also contribute to the net charge. Because the charge on these ionizable groups is pH dependent, the net charge of a protein varies with the pH of its environment. Thus a protein can be negative, neutral or positive in charge depending upon the pH of the solution in which it is