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Dive into the research topics where Marion Waller is active.

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Featured researches published by Marion Waller.


Experimental Biology and Medicine | 1956

Use of Anti-Rh Sera for Demonstrating Agglutination Activating Factor in Rheumatoid Arthritis.

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

Sjögren's Syndrome: Hyperviscosity and Intermediate Complexes

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

Immunochemical and serological studies of enzymatically fractionated human IgG glubulins—I: Hydolysis with pepsin, papain, ficin and bromelin

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

Connective-Tissue Disease and Rheumatoid Factors in Patients with Renal Transplants

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

Immunochemical and serological studies of enzymatically fragmented human IgG globulins—II: Hydrolysis with subtilisin, elastase, trypsin, and chymotrypsin

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

NEW SERUM GROUP, GM(P).

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

Nephelometric method for determination of rheumatoid factor

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

SEROLOGICAL STUDIES OF ENZYMATICALLY FRAGMENTED IgG GLOBULINS

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

Linkage studies of genes for sickling and MNS blood groups; negative findings.

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

The association of the serum agglutinators with the feast IgG globulins

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.

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H. Hugh Fudenberg

Medical University of South Carolina

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