Marion Waller
VCU Medical Center
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Marion Waller.
Experimental Biology and Medicine | 1956
Marion Waller; John H. Vaughan
Conclusions It has been shown that certain anti-Rh sera can be utilized to sensitize Rh positive cells to the agglutination activating factor (AAF) in rheumatoid arthritis sera. The reaction depends upon some characteristic of anti-Rh sera other than titer alone. The possibility is supported that AAF may be a multicomponent system consisting either of multiple antibodies or of a single antibody with multiple cross specificities.
Annals of Internal Medicine | 1974
William M. Blaylock; Marion Waller; David E. Normansell
Abstract A patient with Sjogrens syndrome who developed hyperviscosity is described. A polyclonal increase in all immunoglobulins was present, and ultracentrifuge studies showed the presence of in...
Immunochemistry | 1968
Marion Waller; Nellie Curry; Jean Mallory
Abstract Ummunochemical methods are not available to distinguish the Fab fragments of IgG glubulins produced by a variety of proteolytic enzymes. Serum agglutinators (anti-γ-globulin antibodies) are present in most human sera, in sufficient titer with serologic specificity for these different Fab fragments. They permit a differentiation of the Fab fragments surpassing in sensitivity the available immunochemical methods.
The New England Journal of Medicine | 1965
Marion Waller; Robert Irby; Franklin Mullinax; Elam Toone
AN impressive body of experimental evidence can be summarized by the statement that graft rejection is initiated by an immunologic process.1 Similarly, there is evidence that immunologic events may...
Immunochemistry | 1969
Marion Waller; Alfred J. Richard; Jean Mallory
Abstract Fragmentation of the IgG globulins of a single anti-Rh serum by trypsin, chymotrypsin, subtilisin and elastase is compared to previous studies using papain, pepsin, ficin and bromelin. Natural antibodies in human sera are able to differentiate the Fab fragments produced by the different enzymes.
Science | 1963
Marion Waller; Roscoe D. Hughes; J. Ives Townsend; Edward C. Franklin; H. Hugh Fudenberg
The agglutination that occurs when rheumatoid arthritis serum Pond is added to erythrocytes sensitized with anti-D serum Moore is inhibited in the presence of some normal serums. The inhibitor, tentatively named Gm(p), is associated only with 7S gamma globulins and is apparently different from other previously defined serum groups. It is much more common in Caucasians than in Negroes, and probably is determined by a simple dominant gene.
Journal of Immunological Methods | 1978
Gabriel Virella; Marion Waller; H. Hugh Fudenberg
We have developed a nephelometric technique for determining titers of rheumatoid factor. Serum dilutions are added to a mixture of commercially available latex particles of small size (0.098 micrometer) and human gamma-globulin. Rheumatoid sera induce a substantial increase in the light scattering properties of the mixture, and the highest dilution significantly increasing the light scattering is considered as the titer for that serum. This technique is simple to use, provides objective results, and can be automated for analysis of large numbers of samples.
Human Anti-Human Gammaglobulins#R##N#Their Specificity and Function | 1971
Marion Waller
Publisher Summary This chapter discusses serological studies of enzymatically fragmented IgG globulins. A study was undertaken to demonstrate that the Fab agglutinators will restore to the Fab fragment of a complement binding hemagglutinating antibody, the ability to bring about immune hemolysis. A complement binding rabbit anti-human erythrocyte antibody hydrolyzed with papain and rabbit papain agglutinators were used for this study because it was difficult to obtain a comparable human system. The chapter shows the result of this study. The immune rabbit serum showed both IgG and IgM anti-erythrocyte antibodies. However, only the IgM antibody caused hemolysis of the erythrocytes. Two normal rabbit sera were selected, one with a very high titer of papain agglutinators and one with very little papain agglutinator activity. The IgG fraction of the immune rabbit serum was hydrolyzed with papain and it was demonstrated that the Fab fragments readily coated the human red blood cells. The Fab-coated cells were hemolyzed in the presence of IgM papain agglutinators but not in the presence of the IgG agglutinator although the IgG agglutinator clumped the coated cells. There was no hemolysis when the whole serum of a non-agglutinator rabbit was substituted for the IgM agglutinator.
Experimental Biology and Medicine | 1952
Marion Waller; Robert K. Waller; Roscoe D. Hughes
Summary Analysis of data supplied by 55 Negro families comprising 325 kindred, failed to reveal linkage between the MNS blood group genes and the gene for sickling. These findings are not in accord with those of Snyder and coworkers. Thus an example of autosomal linkage, for which Snyder et al. presented evidence, is now in doubt and warrants further investigation. Data ascertainable for linkage calculations between the blood group S and sickling, and MN and S were very small. Linkage between S and sickling could not be found. The blood groups MN and S afforded evidence for linkage thus fitting into the very considerable evidence on this point for Caucasians.
Immunochemistry | 1973
Marion Waller; C.E. Moncure
Abstract Although anti-Rh antibodies have been shown to be produced as slow IgG globulins, the serum agglutinators (antibodies to IgG Fab fragments) are usually produced as fast IgG globulins, and this is especially true when they are demonstrable in high titer in patients with severe suppurative infection.