N-TERMINAL GROUPS OF NORMAL HUMAN GAMMA GLOBULIN AND OF MYELOMA PROTEINS

1953 ◽  
Vol 75 (11) ◽  
pp. 2785-2786 ◽  
Author(s):  
Frank W. Putnam
Keyword(s):  
Gamma Globulin ◽  
Myeloma Proteins ◽  
Normal Human ◽  
Human Gamma Globulin

scholarly journals BLOOD FACTOR IN ACUTE DISSEMINATED LUPUS ERYTHEMATOSUS

Blood ◽  
1950 ◽  
Vol 5 (8) ◽  
pp. 718-722 ◽  
Author(s):  
JOHN R. HASERICK ◽  
LENA A. LEWIS
Keyword(s):  
Bone Marrow ◽  
Human Serum ◽  
Lupus Erythematosus ◽  
Gamma Globulin ◽  
Normal Human Serum ◽  
Rabbit Serum ◽  
Supernatant Fluid ◽  
Distinct Component ◽  
Normal Human ◽  
Human Gamma Globulin

Abstract The gamma globulin fractionated by the Tiselius electrophoretic technic from the plasma of patients with acute disseminated lupus erythematosus was used as an antigen to induce antibodies in rabbits. Similarly, antibodies were induced in control rabbits with normal human serum and with normal human gamma globulin. The antisera developed in these three groups of rabbits were added to the L. E. gamma globulin solution and, after precipitation, the supernatant fluid was added to bone marrow preparations. The L. E. phenomenon was not demonstrable after the L. E. gamma globulin was precipitated by anti-L. E. gamma globulin rabbit serum. However, after precipitation of the L. E. gamma globulin by anti-normal human serum rabbit serum, or by anti-normal human gamma globulin rabbit serum, the L. E. phenomenon was still apparent. These studies suggest that the L. E. factor is an immunologically distinct component of L. E. gamma globulin.

scholarly journals Chronic Lymphocytic Leukemia, Hypogammaglobulinemia and Autoimmune Hemolytic Anemia— An Experiment of Nature

Blood ◽  
1960 ◽  
Vol 15 (5) ◽  
pp. 748-757 ◽  
Author(s):  
ANTHONY V. PISCIOTTA ◽  
LOUIS F. JERMAIN ◽  
JEAN E. HINZ
Keyword(s):  
Hemolytic Anemia ◽  
Autoimmune Hemolytic Anemia ◽  
Gamma Globulin ◽  
Lymphocytic Leukemia ◽  
Chronic Lymphatic Leukemia ◽  
Lymphatic Leukemia ◽  
Normal Human ◽  
Human Gamma Globulin

Abstract 1. The case study is presented of a 75 year old man who had chronic lymphatic leukemia, autoimmune hemolytic anemia and hypogammaglobulinemia. The positive antiglobulin reaction with serum made from gamma globulin and the neutralization of the antiglobulin reaction with human gamma globulin demonstrated that this patient’s erythrocytes were coated with gamma globulin. 2. There was a normal survival time of I131-labeled normal human gamma globulin, suggesting defective synthesis of gamma globulin. Failure to demonstrate radioactivity on the patient’s erythrocytes when I131-labeled normal gamma globulin was given signified that normal human gamma globulin has no affinity in vivo for the patient’s red cells and that the erythrocyte-coating protein was derived from a source endogenous to the patient. 3. These relationships favor an immunologic mechanism in the development of an antiglobulin reaction in this patient.

scholarly journals Protection of Nonimmune Volunteers against Rubella by Intravenous Administration of Normal Human Gamma Globulin

1972 ◽  
Vol 126 (3) ◽  
pp. 341-344 ◽  
Author(s):  
R. Martin du Pan ◽  
B. Koechli ◽  
A. Donath
Keyword(s):  
Intravenous Administration ◽  
Gamma Globulin ◽  
Normal Human ◽  
Human Gamma Globulin

scholarly journals IMMUNOLOGIC STUDIES WITH ETHYLENE OXIDE-TREATED HUMAN SERUM

1961 ◽  
Vol 113 (6) ◽  
pp. 1029-1040 ◽  
Author(s):  
Paul H. Maurer
Keyword(s):  
Ethylene Oxide ◽  
Human Serum ◽  
Gamma Globulin ◽  
Serum Proteins ◽  
Skin Testing ◽  
Tuberculin Reaction ◽  
The Poor ◽  
Normal Human ◽  
Human Gamma Globulin ◽  
Autoimmune Phenomena

The antigenicity of an ethylene oxide-treated human serum in humans has been studied. The immune response to the material had many of the characteristics of a delayed cellular skin reaction. Even after repeated immunizations by intradermal skin testing over a period of 1½ years, no detectable antibody could be found in the sera. The antigenicity has been shown to be associated with drastic alteration of the homologous serum proteins as evidenced by (a) the formation of new proteins, and (b) the poor cross-reactions of the modified serum proteins with antisera against normal human serum albumin and normal human gamma globulin. The delayed hypersensitivity was transferable to normal recipients by either viable or killed leukocytes. The implications of these findings have been discussed with respect to the problem of sterilization of sera, the tuberculin reaction, and autoimmune phenomena.

Subfractions of Human Gamma Globulin as Reactant in the Latex Fixation Test

1959 ◽  
Vol 5 (1) ◽  
pp. 12-17 ◽  
Author(s):  
H. Hedberg ◽  
U. Moritz
Keyword(s):  
Gamma Globulin ◽  
Fixation Test ◽  
Human Gamma Globulin

scholarly journals Antibody Prophylaxis and Therapy against West NileVirus Infection in Wild-Type and ImmunodeficientMice

2003 ◽  
Vol 77 (24) ◽  
pp. 12941-12949 ◽  
Author(s):  
Michael J. Engle ◽  
Michael S. Diamond
Keyword(s):  
B Cell ◽  
Gamma Globulin ◽  
Polyclonal Antibodies ◽  
Current Treatment ◽  
Mouse Serum ◽  
Wild Type ◽  
Viral Reservoirs ◽  
In The Wild ◽  
Human Gamma Globulin ◽  
Immune Antibody

ABSTRACT West Nile virus (WNV) is a mosquito-borne Flavivirus that causes encephalitis in a subset of susceptible humans. Current treatment for WNV infections is supportive, and no specific therapy or vaccine is available. In this study, we directly tested the prophylactic and therapeutic efficacy of polyclonal antibodies against WNV. Passive administration of human gamma globulin or mouse serum prior to WNV infection protected congenic wild-type, B-cell-deficient (μMT), and T- and B-cell-deficient (RAG1) C57BL/6J mice. Notably, no increased mortality due to immune enhancement was observed. Although immune antibody completely prevented morbidity and mortality in wild-type mice, its effect was not durable in immunocompromised mice: many μMT and RAG1 mice eventually succumbed to infection. Thus, antibody by itself did not completely eliminate viral reservoirs in host tissues, consistent with an intact cellular immune response being required for viral clearance. In therapeutic postexposure studies, human gamma globulin partially protected against WNV-induced mortality. In μMT mice, therapy had to be initiated within 2 days of infection to gain a survival benefit, whereas in the wild-type mice, therapy even 5 days after infection reduced mortality. This time point is significant because between days 4 and 5, WNV was detected in the brains of infected mice. Thus, passive transfer of immune antibody improves clinical outcome even after WNV has disseminated into the central nervous system.

scholarly journals Effects of Adrenocorticotropin and Dietary Ascorbic Acid on Delayed Type Hypersensitivity to Human Gamma Globulin in Chickens

1987 ◽  
Vol 66 (11) ◽  
pp. 1859-1869 ◽  
Author(s):  
D.L. MURRAY ◽  
J. BRAKE ◽  
J.P. THAXTON ◽  
R.P. GILDERSLEEVE
Keyword(s):  
Ascorbic Acid ◽  
Gamma Globulin ◽  
Delayed Type Hypersensitivity ◽  
Human Gamma Globulin

ANTIBODIES IN HUMAN GAMMA GLOBULIN

1953 ◽  
pp. 174-179 ◽  
Author(s):  
JOHN F. ENDERS
Keyword(s):  
Gamma Globulin ◽  
Human Gamma Globulin

Use of polyethylene glycol in separating bound from unbound ligand in radioimmunoassay of thyroxine.

1976 ◽  
Vol 22 (3) ◽  
pp. 299-304 ◽  
Author(s):  
M C Cheung ◽  
W R Slaunwhite
Keyword(s):  
Polyethylene Glycol ◽  
Human Serum ◽  
Salt Concentration ◽  
Room Temperature ◽  
Gamma Globulin ◽  
Separation Process ◽  
Normal Human Serum ◽  
Normal Sheep Serum ◽  
Normal Human ◽  
Entire Procedure

Abstract In most rapid radioimmunoassay methods, absorbents are used that disturb the equilibrium of the ligand-antibody interaction; thus the separation process must be rigidly timed. We show here that polyethylene glycol (mol wt. 6000) abolishes this constant. We measured gamma-globulin precipitation by polyethylene glycol (150g/liter) in a thyroxine radioimmunoassay system involving use of a sheep anti-thyroxine antiserum, quantitatively and qualitatively, with either normal human serum or completely precipitated at pH 6-9 at 4 and 25 degrees C, but incompletely if salt concentration was high (1 mol/liter). Specificity of gamma-globulin precipitation increased with increasing pH and temperature. All gamma-globulin-bound thyroxine was precipitated, and also some not bound to gamma-globulin. This was taken into account by including "blank" tubes (no antibody, but with normal sheep serum) in all assays. Because this reaction is predominantly entropic and temperature independent, the entire procedure can be done at 37 degrees C and room temperature without rigid timing. The assay requires 10 mul of serum, its reproducibility is 4-8% (CV) in the euthyroid and hyperthyroid range, and its accuracy is close to 100%.

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