PubMed Health⌕ Search

Biomedical subjects

R F JACOX

Publications and source records attributed to R F JACOX.

At least 19 recordsLinked to original sources
PubMed1961

Cellular source and charcter of a heatstable bactericidal property associated with rabbit and rat platelets.

Rabbit and rat platelets contain two non-dialyzable components (analogous to Myrvik's components 1 and 2 of serum) which, together with bicarbonate ions, produce a potent bactericidin for B. subtilis. These platelet factors appear to be identical with the serum bactericidal substances, suggesting that disruption of platelets during blood coagulation releases the platelet factors into serum. Normal human platelets contain no measurable component 1 or 2. Since bovine serum contains component 2 but little or no component 1, estimation of the concentration of component 1 in sera or platelet suspensions of other species can be made by diluting the materials to be tested in bovine serum. The level at which a bactericidal effect is lost represents the end-point of the titration of component 1. Rabbit serum has a high concentration of component 1 and a lower concentration of component 2. It can be diluted to a point at which bactericidal activity is lost, owing to a depletion of component 2, but at which component 1 is still present in effective concentration. At this point the addition of another serum or a platelet homogenate causes a restoration of the bactericidal activity and permits an estimate of the concentration of component 2 in the added material.

Animals↗
PubMed1959

Analysis of the proteins of rat serum by starch electrophoresis and by cationic detergent analysis. I. Identification of an unusual globulin.

A protein of unusual characteristics has been identified in normal rat sera by electrophoretic separation at pH 8.6, followed by precipitation of each fraction with a cationic detergent. This protein, which is closely identified with albumin after electrophoresis at pH 8.6, precipitates with cationic detergent at a low pH in contrast to albumin which precipitates with detergent only at a high pH. This protein has characteristics of a globulin and is designated as a "fast alpha fraction." This fraction and albumin are present in about equal amounts in sera of normal rats. A separation of the fast alpha fraction can be made by electrophoresis in an acetate buffer of pH 4.25 and by precipitation according to a modified Cohn, cold-alcohol technique. A protein of similar characteristics has not been found in either human or rabbit sera studied by the same method of electrophoresis and subsequent sub-fractionation with cationic detergent.

Animals↗
PubMed1956

A study of plasma protein alterations in rabbits infected with type I pneumococci.

An investigation of the plasma protein changes in rabbits infected intradermally with Type I pneumococci has been carried out, utilizing a cationic detergent method of protein fractionation. A consistent pattern of change was observed. There was an increase in the alpha globulins and fibrinogen concentration which reached maximal levels at the height of the infection. Albumin fell to a minimal concentration when the increment of alpha globulins and fibrinogen was greatest. The beta-gamma concentration showed a significant decrease during the most severe phase of the infection but returned to normal several days after spontaneous subsidence of bacteremia. The magnitude of these plasma protein alterations depended on the severity of the infection and the response of the host. Significantly greater changes were observed in rabbits severely bacteremic than in those with mild bacteremia. Administration of penicillin suppressed the infection and decreased the usual plasma protein alterations. Injection of cortisone prior to the onset of the Type I pneumococcus infection caused an early inhibition of the expected plasma protein changes, but later the protein pattem developed in the same manner as it did in the severely infected animals.

Animals↗