Immunochemical studies on human plasma lipoproteins

Some years ago, a series of human serum lipoproteins, distinguishable by their hydrated densities and lipid-protein ratios were recognized and isolated by ultracentrifugal techniques (1). Certain of these lipoproteins are invariably present in human serum and the concentrations of these and of others can be quantitatively correlated with disease (2). No difference in the lipoprotein distribution can be demonstrated between serum and plasma. The purpose of this investigation was to obtain information about the immunochemical specificity of some of the lipoproteins

Protein concentration of synovial fluid in chronic rheumatoid arthritis. Estimation of protein in the synovial fluid of chronic rheumatoid arthritis by gel filtration and paper electrophoresis

For the purpose to reveal the characteris6cs of the synovial fluid of the chronic rheumatoid arthritis the proteins of the synovial fluid and blood serum have been analysed by employing the methods of electrophoresis, gel filtration on Sephadex G-200 column and ultracentrifugation. Waaler-Rose test and latex fixation test have also been made on each protein fraction, and the following results were obtained. 1) The total protein level of synovial fluid, which is 3/5 of that of the serum, is slightly higher than that of control. 2) Fractionation of the synovial proteins by electrophoresis revealed nearly the same protein contents in each fraction in percentage as that of comparable fraction of the serum protein, with a slight increase in &#947;-globulin fraction. 3) The fractionation by Sephadex column G-200 give three peaks both in serum and synovial fluid, 19 S, 7Sand 4S. 4) 19S fraction of the synovial fluid, which is mainly of &#947;-globulin, showed a higher level than that of the synovial fluid from the controls. 5) Rheumatoid tests gave positive reaction in the 1st peak containing 19S &#947;-globulin from the synovial fluid and blood serum.</p

Competition of haptens

Groups of rabbits were injected with either bovine serum albumin, sheep red cell stroma, or keyhole limpet hemocyanin to which 2,4-dinitrophenyl and/or p-azophenyl arsonate groups had been coupled. Groups of animals received either doubly coupled antigen or an equivalent mixture of singly coupled antigens. Materials were injected intravenously as a solution or subcutaneously and intramuscularly in complete Freund's adjuvant. The presence of dinitrophenyl groups on the immunizing antigen could suppress, partially or completely, the antibody response to p-azophenyl arsonate when this hapten was located on the same molecule. Suppression was dependent on the ratio of haptenic groups on the molecule, appeared to be greatly affected by the method of immunization, and could be demonstrated in all three antigen systems. Partial suppression was manifested in decreased frequency and delayed appearance of the response as well as decreased maximal antibody titers. These findings appear irreconcilable with the possibility of direct clonal selection of antibody-producing cells by unprocessed antigen

The "erythrocyte-coating substance" of "auto-immune" hemolytic disease

Thesis (M.A.)--Boston Universit

Improvements in the preparation of heterologous antilymphocyte globulin with special reference to absorption and diethylaminoethyl cellulose batch production

Antilymphocyte gamma-G globulin (ALGG) was produced from the serum of immunized horses. Modifications of the preliminary absorption techniques permitted the removal of undesirable, extraneous antibodies. With the use of a batch technique, pure gamma-G globulin could then be removed in bulk quantities. The resulting product was first confirmed to have immunosuppressive qualities in dogs and then given a clinical trial. In patients, its administration occasionally caused low-grade fever and thrombocytopenia. Pain at the injection site was not eliminated. Precipitin antibody responses have apparently been prevented in the patients but not a host response to Forssman antigens. © 1969

The retention of S35-labelled bovine serum albumin on normal and immunized rabbit liver tissue

The S35-label of S35-BSA was detected in the liver tissue of rabbits to the extent of 0.02 per cent (10 µg or sime 1014 molecules) of the injected material at 140 days after injection. The rate of loss of antigen at the termination of the experiment was of such an order that significant amounts would be expected to persist for at least several years. Data are reported which extend the retention data previously reported on S35-labelled hemocyanin. They indicate that amounts of the order of 0.05 per cent (25 µg.) of antigen material persist at 330 days after injection. All of the radioactivity of material retained in the liver tissue 6 weeks after injection was immunologically related to the original S35-BSA antigen. Preliminary studies are reported which indicate that the retained antigen is bound to ribonucleic acid. A new method is described for the isolation of p-azophenylsulfonate bovine serum albumin from tissue extracts by means of a Dowex 2 adsorbent

The serlogical specificity of the lectin from Lens culinaris

Lens culinaris, the common lentil, contains a lectin which has been shown to be specific for a glycoprotein saliva antigen and a glycolipoprotein serum antigen. Both the saliva and serum precipitin reactions with the lectin are directly inhibited with saccharides, especially those related to D-mannose. Electrophoresis of the serum antigen showed that it migrates as three bands, while appearing as a single band in double diffusion precipitin patterns. Quantitative studies of the saliva antigen levels by hemagglutination inhibition titration indicated a polygenic, quantitative mode of inheritance with a minimum heritability of O. 34. Blood group ABH secretor individuals were found to have a significantly lower mean saliva antigen level than nonsecretor individuals. The lectins from Pisum sativum and Canavaliafiensiformis formed precipitin bands of identity with L.culinaris lectin against saliva. C. ensiformis and L. culinaris lectins exhibited precipitin bands of partial identity against serum; and P. sativum and L. culinaris lectins exhibited a pattern of identity against serum. In addition, precipitin patterns of partial identity with the non-H lectin from Lotus tetragonolobus has been demonstrated. Using Ulex europaeus lectin in hemagglutination inhibition experiments with saliva from blood group O secretor individuals, a minimum heritability of approximately 0.40 for H antigen levels was found. A higher frequency of nonsecretor individuals was observed in the Black population compared with the White population