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Presents a study on the finding of abnormal protein components in a case of virus hepatitis and Laennec's cirrhosis. Importance of paper electrophoresis to the diagnosis of the disease; Role of paper electrophoresis and chemical fractionation in determining serum protein patterns; Discussion of the abnormal paper electrophoretic components.

1. A new diagonal etectrophoretic technique for determining the order of the lysine-containing tryptic peptides of a protein is described. The protein is converted into its trifluoracetyl derivative, digested enzymatically (or chemically), and the resulting peptides separated by paper electrophoresis. The paper is then treated with ammonia vapour, which re-exposes the ε-amino groups of the lysine residues, and submitted to a second electrophoresis at right angles to the first direction. Peptides containing lysine residues, together with the N-terminal peptide of the protein, are found to lie off a diagonal formed by all other peptides, whence they may be readily purified. A study of these peptides enables the order of the lysine-containing tryptic peptides in the protein to be deduced. 2. The technique has been successfully tested with insulin. 3. When the method was applied to porcine pepsin, the four tryptic peptides isolated were easily ordered and the carboxyl-terminal sequence of the protein shown to be Arg-Gln-Tyr-TyrThr-Val-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ala-Pro-Val-Ala. The thee basic ammo acid residues in the molecule are thus found clustering towards the C-terminus of the polypeptide chain. 4. A common ancestral gene for porcine pepsin and bovine (calf) rennin is suggested by the close homology between the C-terminal sequents of the two proteins. [ABSTRACT FROM AUTHOR]

This article discusses paper electrophoresis patterns of enzymes involved in polyglucoside synthesis in oscillatoria princeps and its low temperature strains. The technique of paper partition chromatography and paper electrophoresis for the study of genetically different tissues have recently found application in the field of genetic studies. These methods should prove of considerable interest in the detection of differences between enzymes having the same properties and functions in the different species.

The article focuses on research into polysaccharide-protein complexes in human gingiva. It states that two polysaccharide-protein complexes with different electrophoretic mobilities were isolated from human gingiva. It mentions that the complexes reacted with the periodic acid-Schiff procedure but were not stained by chondroitin sulfate or hyaluronate. It comments that the polysaccharide portion of the second complex contained several components, including glucuronic acid, glucose, and ribose.