Similarities between IgE in Human Feces and a Chymotrypsin-Digest of an IgE Myeloma Protein

1987 ◽  
Vol 82 (1) ◽  
pp. 100-107 ◽  
Author(s):  
Svein Kolmannskog
Keyword(s):  
Human Feces ◽  
Myeloma Protein ◽  
Ige Myeloma

Structure and Function of IgE Myeloma Protein VL from an Atopic Patient

1996 ◽  
Vol 110 (2) ◽  
pp. 143-148 ◽  
Author(s):  
Vladimír Zavázal ◽  
Vladimír Krauz ◽  
Hartmut Kratzin ◽  
Norbert Hilschmann
Keyword(s):  
Structure And Function ◽  
Myeloma Protein ◽  
Atopic Patient ◽  
And Function ◽  
Ige Myeloma

IMMUNOLOGICAL RELEASE OF HISTAMINE AND SLOW-REACTING SUBSTANCE OF ANAPHYLAXIS FROM HUMAN LUNG

1971 ◽  
Vol 134 (3) ◽  
pp. 136-148 ◽  
Author(s):  
Robert P. Orange ◽  
W. Gerald Austen ◽  
K. Frank Austen
Keyword(s):  
Inhibitory Activity ◽  
Human Lung ◽  
Blocking Agent ◽  
Adrenergic Stimulation ◽  
Temperature Dependent ◽  
Myeloma Protein ◽  
Adrenergic Agents ◽  
Myeloma Proteins ◽  
Ige Myeloma ◽  
Adrenergic Blocking

The sensitization of human lung with atopic serum is both time and temperature dependent. Highly purified IgE myeloma protein is capable of blocking sensitization of human lung with atopic serum whereas myeloma proteins of the IgG subgroups are inactive. Drugs capable of increasing cellular levels of CAMP such as ß-adrenergic agents and methylxanthines inhibit the antigen-induced release of both histamine and SRS-A from human lung and these agents demonstrate synergism when used together. The ß-adrenergic blocking agent, propranolol, prevents epinephrine-induced inhibition of the immunologic release of the mediators. Diethylcarbamazine also inhibits the antigen-induced release of histamine and SRS-A from human lung and a synergism between this drug and epinephrine is observed. Predominantly α-adrenergic stimulation achieved by combining propranolol with epinephrine or norepinephrine not only prevented the inhibitory activity of the sympathomimetic amines but also resulted in an enhanced release of histamine and SRS-A. These observations suggest that whereas increases in cellular levels of CAMP are inhibitory, decreases in cellular levels of CAMP enhance the antigen-induced release of the mediators.

scholarly journals IgE Multiple Myeloma: A Report of the Third Case

Blood ◽  
1972 ◽  
Vol 39 (3) ◽  
pp. 361-367 ◽  
Author(s):  
Ben G. Fishkin ◽  
Natalie Orloff ◽  
Louis E. Scaduto ◽  
David T. Borucki ◽  
Hans L. Spiegelberg
Keyword(s):  
Multiple Myeloma ◽  
Iliac Crest ◽  
Clinical Manifestations ◽  
Specific Ige ◽  
Surgical Biopsy ◽  
Myeloma Protein ◽  
The Third ◽  
Light Chain Type ◽  
Ige Myeloma ◽  
Chain Type

Abstract The third known case of IgE multiple myeloma is described. The patient was a 65-yr-old woman who died 11 mo after a diagnosis of multiple myeloma was made by a surgical biopsy of the left iliac crest. Her serum contained approximately 2.7 g/100 ml of a paraprotein of mid-γ mobility. The isolated anomalous protein gave a reaction of identity with the IgE myeloma protein of the second reported case when reacted with a specific IgE antiserum. The light-chain type of the myeloma protein was κ in contrast to λ of the other two IgE myeloma proteins. Her clinical manifestations differed from the two previously reported cases in several respects. She had neither plasma cell leukemia nor overt Bence Jones proteinuria and developed rapidly progressive widespread osteosclerotic lesions that were associated with bone pain.

scholarly journals ELECTRON MICROSCOPIC LOCALIZATION OF IMMUNOGLOBULIN E ON THE SURFACE MEMBRANE OF HUMAN BASOPHILS

1971 ◽  
Vol 134 (6) ◽  
pp. 1403-1416 ◽  
Author(s):  
Albert L. Sullivan ◽  
Philip M. Grimley ◽  
Henry Metzger
Keyword(s):  
Room Temperature ◽  
Immunoglobulin E ◽  
Surface Membrane ◽  
Human Leukocyte ◽  
Electron Microscopic ◽  
Myeloma Protein ◽  
Ige Myeloma ◽  
Human Basophils ◽  
Hybrid Antibody ◽  
Electron Microscopic Localization

We have examined human leukocyte preparations for the presence of surface-bound IgE by electron microscopy. Basophil-enriched leukocytes were reacted with burro anti-IgE, a hybrid antibody to burro IgG and ferritin, and ferritin, with or without prior incubation of the cells with an IgE myeloma protein. In the absence of preincubation with IgE small amounts of ferritin were fixed to the surface of basophils but on no other cells. When cells were preincubated with IgE the amount of ferritin fixation on the basophils was markedly increased and a small amount of ferritin was also bound to platelets but again to no other leukocytes. The distribution of ferritin on the basophil surface appeared dependent upon the temperature at which the cells were kept during and after reaction with the various reagents. Basophil sections from cells kept at 0°C had ferritin bound to the surface membrane in patches distributed around the entire circumference. Basophil sections from cells prepared at room temperature had ferritin distributed assymetrically covering a surface membrane segment one-fifth to one-half of the circumference. In control studies in which monomeric IgG was substituted for the IgE and burro anti-IgG was used instead of burro anti-IgE, no cellular fixation of ferritin was observed.

Macroglobulinemia: The Usefulness of DL-Penicillamine and Paper Electrophoresis in Diagnosis

1964 ◽  
Vol 10 (7) ◽  
pp. 600-605 ◽  
Author(s):  
Donald J Campbell ◽  
Thomas Boenisch
Keyword(s):  
Paper Electrophoresis ◽  
Myeloma Protein

Abstract The change in mobility of an abnormal globulin peak during paper electrophoresis in the presence of DL-penicillamine is the most useful of simple procedures suggested for differentiation between macroglobulin and myeloma protein. However, not all cases indicating macroglobulin by this procedure will correlate with criteria based on ultracentrifuge analysis or antigenic reaction.

scholarly journals Recovery of SARS-CoV-2 from Wastewater Using Centrifugal Ultrafiltration

2021 ◽  
Vol 4 (2) ◽  
pp. 32
Author(s):  
Brienna L. Anderson-Coughlin ◽  
Adrienne E. H. Shearer ◽  
Alexis N. Omar ◽  
K. Eric Wommack ◽  
Kalmia E. Kniel
Keyword(s):  
Enteric Virus ◽  
Clinical Testing ◽  
Human Feces ◽  
Angiotensin Converting Enzyme 2 ◽  
Human Waste ◽  
Safety Research ◽  
New Castle County ◽  
Wastewater Systems ◽  
High Concentrations ◽  
Centrifugal Ultrafiltration

The COVID-19 pandemic is a global crisis and continues to impact communities as the disease spreads. Clinical testing alone provides a snapshot of infected individuals but is costly and difficult to perform logistically across whole populations. The virus which causes COVID-19, SARS-CoV-2, is shed in human feces and urine and can be detected in human waste. SARS-CoV-2 can be shed in high concentrations (>107 genomic copies/mL) due to its ability to replicate in the gastrointestinal tract of humans through attachment to the angiotensin-converting enzyme 2 (ACE-2) receptors there. Monitoring wastewater for SARS-CoV-2, alongside clinical testing, can more accurately represent the spread of disease within a community. This protocol describes a reliable and efficacious method to recover SARS-CoV-2 in wastewater, quantify genomic RNA levels, and evaluate concentration fluctuations over time. Using this protocol, viral levels as low as 10 genomic copies/mL were successfully detected from 30 mL of wastewater in more than seven-hundred samples collected between August 2020 and March 2021. Through the adaptation of traditional enteric virus methods used in food safety research, targets have been reliably detected with no inhibition of detection (RT-qPCR) observed in any sample processed. This protocol is currently used for surveillance of wastewater systems across New Castle County, Delaware.

Coprobacter secundus subsp. similis subsp. nov. and Solibaculum mannosilyticum gen. nov., sp. nov., isolated from human feces

2021 ◽  
Author(s):  
Mitsuo Sakamoto ◽  
Nao Ikeyama ◽  
Atsushi Toyoda ◽  
Takumi Murakami ◽  
Hiroshi Mori ◽  
...  
Keyword(s):  
Human Feces
Sign in / Sign up

Export Citation Format

Share Document