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Biomedical subjects

E C FRANKLIN

Publications and source records attributed to E C FRANKLIN.

At least 55 records · Page 3Linked to original sources
PubMed1959

Comparative studies on the physical characteristics of the heritable haptoglobin groups of human serum.

Ultracentrifugal studies of the alpha(2)-proteins of normal human serum before and after the addition of hemoglobin have revealed three separate and clearly distinguishable patterns based on the three major serum haptoglobin groups. Isolation of the three haptoglobin hemoglobin complexes disclosed characteristic patterns for each group. The heterozygote was found to possess electrophoretic and ultracentrifugal components not seen in either homozygote. Separation of normal human serum, to which hemoglobin had been added, by conventional starch zone electrophoresis resulted in three characteristic patterns which also permitted the ready identification of the serum haptoglobin group. The haptoglobin hemoglobin complex from Group 1-1 had the fastest mobility and that of Group 2-2 the slowest. The heterozygote Group 2-1 had an intermediate mobility. Immunologic differences between the haptoglobin hemoglobin complexes of the three groups could not be detected. Some of the variations in the reported electrophoretic and ultracentrifugal patterns of normal human serum could be reasonably ascribed to the group variation of the haptoglobins in man. The physical studies imply that the proteins characteristic of the heterozygote differ in size and charge from those present in either of the two homozygotes and indicate that the genetic control of the synthesis of the serum haptoglobins is probably exceedingly complex.

Blood Proteins↗
PubMed1958

Interaction of the rheumatoid factor with antigen-antibody complexes and aggregated gamma globulin.

The effect of highly purified rheumatoid factor on the precipitin reactions of various antigen-antibody systems was determined. The amount of nitrogen precipitated was increased over a broad range when the factor was added to ovalbumin, human albumin, or human gamma globulin, and the corresponding rabbit antibodies. In the zone of antigen excess, soluble antigen-antibody complexes were precipitated by rheumatoid factor. Soluble aggregates of human and rabbit gamma globulin, produced by heating at 63 degrees C., treatment with urea plus mercaptoethanol or treatment with guanidine, also precipitated with rheumatoid factor. Ultracentrifugal analysis of dissolved specific precipitates showed the presence of aggregated gamma globulin. The sedimentation rate of reactive aggregates was greater than 20 S, and concentrated preparations free of the non-reactive 7 S gamma globulin could be prepared by various procedures of zone centrifugation. These aggregates showed a high inhibitory capacity in the sensitized sheep cell agglutination reaction. Solid gamma globulin, prepared by heat denaturation, also selectively adsorbed the rheumatoid factor, and removed or decreased the activity in the various precipitation and agglutination reactions. Elution of highly purified active preparations from the solid gamma globulin could be carried out with urea or acid buffers. Evidence for interaction between rheumatoid factor and low molecular weight gamma globulin without precipitation, was also obtained. This interaction appears to occur in the circulation of patients with rheumatoid arthritis. The question of whether the rheumatoid factor represents an antibody to gamma globulin was discussed. Points of similarity to the behavior of complement also were cited.

Animals↗
PubMed1957

An unusual protein component of high molecular weight in the serum of certain patients with rheumatoid arthritis.

In the sera of a number of patients with rheumatoid arthritis an unusual, high molecular weight protein component could be detected by direct ultracentrifuge analysis of whole serum. This material sedimented more rapidly than the normal 19 S component and reached concentrations up to 340 mg. per cent. Similar components were not observed in a limited control series. The high molecular weight material was present in the gamma-globulin fraction of serum and joint fluid. It had an S20,(w) of approximately 22 S and could be dissociated into 2 fractions, one of which had a sedimentation coefficient of approximately 19 S. Evidence for a direct relationship between the 22 S component and the gamma-globulin precipitation test was obtained. The latter reaction was found to occur in the presence of altered, aggregated gamma globulin. Absorption of serum with altered gamma globulin removed the 22 S component. There also appeared to be a connection with the sheep cell agglutination reaction and the latex fixation test. The 22 S fraction was always observed in sera giving the most positive tests. Procedures of density gradient and repeated preparative ultracentrifugation demonstrated that each of these reactions was caused by a high molecular weight fraction. The relationship between the unusual protein complex and various 19 S gamma-globulins and 19 S antibodies is discussed.

Arthritis, Rheumatoid↗