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Serum α1-antitrypsin, α1-acid glycoprotein, baptoglobin, ceruloplasmin and C-reactive protein are increased, albumin, transferrin, α1-and β-lipoprotein are decreased as an early response to tissue trauma and inflammatory disease. In infection these changes are followed by a rise of γ-globulins.

SUMMARY The survival of rabbit skin allografts was significantly prolonged for up to 22 days following treatment of the skin grafts with electrophoresis prior to transplantation. No relationship between one combination of current and time and a maximum survival time could be established. A new method of window electrophoresis is presented, and its possible advantages over regular paper electrophoresis are discussed.

Paper disc-electroimmunodiffusion in agarose gel provides a rapid and sensitive quantitation of the immunoprecipitin reaction.

An acidic polysaccharide was isolated from wild type (K+) Escherichia coli 09:K29 (A) but could not be isolated from an uncapsulated (K−) mutant of this strain. Analytical ultracentrifugation showed that the polysaccharide was physically heterogeneous but became homogeneous when treated with alkali. Alkali treatment also reduced the viscosity of aqueous solutions of the polysaccharide, while other physical properties were not affected. The molecular weight of the alkali-treated acidic polysaccharide is 332000, as calculated from s20 (4.7 × 1013 sec) and D20 (1.08 nm/sec). The polysaccharide consists of glucose, mannose, galactose and glucuronic acid in the molar ratios of 2:2:1:1. It also contains an acid labile substituent which was tentatively identified as pyruvate. After partial hydrolysis 7 oligosaccharides were isolated and analyzed. Oligosaccharide analysis, together with the results of methylation, periodate oxidation and carboxyl reduction indicated that the acidic polysaccharide consists of the hexasaccharide repeating unit The glycsoidic bond between the repeating units is an α-galactosyl-(1,6)-mannose linkage. The alkali-treated acidic polysaccharide represents a subunit chain with a length of about 300 repeating units. It is suggested that these subunit chains are interlinked by alkali labile ester bonds between the carboxyl group of glucuronic acid residues and hydroxyl groups in the chains. With the aid of passive haemagglutination and immune precipitation in O-, OK-, and K sera and with bacterial agglutination in OK serum before and after absorption with the acidic polysaccharide it was shown that the acidic polysaccharide represents the K29 antigen. Serological studies with chemically altered polysaccharide preparations indicated that glucuronic acid and mannose are immunodominant sugar residues. Inhibition of the K29 specific precipitin reaction with oligosaccharides obtained from the K29 polysaccharide and with the degraded polysaccharides of Salmonella anatum and Salmonella newington indicated that the determinant region of the K29 antigen is represented by the trisaccharide Man, which is probably partially substituted by pyruvate.

1. (1) The solubility of purified low density lipoprotein in the presence of various concentrations of a clinical dextran preparation (mean mol. wt. 71400) has been investigated at physiological pH and ionic strength. 2. (2) Dextran concentrations above 7% (w/v) caused precipitation of low density lipoprotein from a solution containing 1.1% (w/v) of the protein. 3. (3) The results have been explained in terms of an activity increment of low density lipoprotein due to steric exclusion by dextran. 4. (4) The activity increment caused by 1% dextran has been calculated and is approximately 50%.

It has been proposed that particles within tubules and vesicles of the Golgi apparatus of liver cells are precursors of very low density lipoproteins in blood plasma. To characterize these particles we isolated a cell fraction rich in Golgi apparatus and associated particles from rat liver in quantities sufficient for analysis. Particles freed from the membranes of the Golgi apparatus and floated at d = 1.006 were studied by chemical analysis, immunodiffusion, and paper electrophoresis. The lipid composition of the Golgi particles was similar to that of very low density lipoproteins from the same rats. The protein content was about 10% of dry weight for both the Golgi particles and plasma very low density lipoproteins. The Golgi particles formed lines of identity with plasma very low density lipoproteins during immunodiffusion against antiserum to plasma very low density lipoproteins. On paper electrophoresis, however, many Golgi particles remained near the origin, with only a few migrating to the pre-beta position. It was concluded that the lipoproteins in the Golgi apparatus are the precursors of plasma very low density lipoproteins.

The structural determinants for antigen 34 in the E group salmonella are glucosyl substituents on the galactosyl units of the O antigen which has a mannosylrhamnosylgalactose repeating sequence. The temperate bacteriophage ε 34 brings about the production of antigen 34. It has been shown here that glucose is transferred from uridine diphosphate glucose to the O antigen via a glucosyl-lipid intermediate in a two-step reaction. Glucose is linked through carbon 1 to the lipid by a phosphodiester bridge, the glucosyl bond having the β-anomeric configuration. The lipid is a C 55 -polyisoprenoid alcohol, each isoprene unit having one double bond. It is the same lipid which is involved in the synthesis of the O antigen repeating sequence.

Immunoelectrodiffusion with paper discs is a simple and rapid method for screening blood donors for hepatitis antigen.