scholarly journals Sickle Hemoglobin: A Specific Radioimmunoassay

Blood ◽  
1974 ◽  
Vol 43 (4) ◽  
pp. 607-611 ◽  
Author(s):  
Peter T. Rowley ◽  
Richard A. Doherty ◽  
Cheryl Rosecrans ◽  
Elsa Cernichiari
Keyword(s):  
Gamma Globulin ◽  
Adult Type ◽  
Hemoglobin S ◽  
Hemoglobin A ◽  
Specific Radioimmunoassay ◽  
Highly Sensitive ◽  
Antibody Complex ◽  
Chloramine T ◽  
Antigen Antibody ◽  
Complete Precipitation

Abstract For the quantitation of hemoglobin S, a radioimmunoassay has been developed which is specific and highly sensitive. Hemoglobin S was purified by column chromatography and injected with complete Freund’s adjuvant into goats. Each goat serum was tested for reactivity against hemoglobins A and S by immunodiffusion and by quantitative precipitation. Hemoglobin A reactivity was removed by absorption with hemoglobin A. One serum so treated was specific for hemoglobin S; it reacted negligibly with hemoglobins A or F. Hemoglobin S was labeled with 125I by the chloramine T method. In the radioimmunoassay, complete precipitation of the antigen—antibody complex was insured by the addition of rabbit antigoat gamma globulin. This assay offers reliable and specific quantitation of as little as 1 ng of hemoglobin S. Assuming that 10% of the hemoglobin in fetal blood at 16 wk gestation is of adult type, this assay is capable of detecting the amount of hemoglobin S in 10-7 ml of homozygous hemoglobin S blood. The prenatal diagnosis of sickle cell anemia by radioimmunoassay will require, in addition, a method for demonstrating the absence of hemoglobin A and a safe method for obtaining fetal erythrocytes without significant contamination by maternal erythrocytes.

Application of Radioimmunoassay for Detection of Staphylococcal Enterotoxins in Foods

1980 ◽  
Vol 43 (1) ◽  
pp. 68-72 ◽  
Author(s):  
MERLIN S. BERGDOLL ◽  
RAOUL REISER
Keyword(s):  
Solid Phase ◽  
Protein A ◽  
Staphylococcal Enterotoxins ◽  
A Cells ◽  
Low Concentrations ◽  
Antibody Complex ◽  
Chloramine T ◽  
Antigen Antibody

The staphylococcal enterotoxins can be iodinated with chloramine-T, lactoperoxidase or gaseous iodine. Low concentrations of enterotoxin, chloramine-T and 125I are recommended to avoid possible damage to the enterotoxin. The antigen-antibody complex can be separated from the unreacted enterotoxin by antibodies adsorbed onto tubes or bromoacetyl-cellulose or by precipitation of the complex with a second antibody or protein A cells. As little as 1 ng of enterotoxin per gram of food can be detected in food extracts with the solid-phase tube method or by precipitation of the antigen-antibody complex with protein A cells.

Double-antibody radioimmunoassay for staphylococcal enterotoxins A and B

1978 ◽  
Vol 24 (4) ◽  
pp. 436-439 ◽  
Author(s):  
Haskel Robern ◽  
Thomas M. Gleeson ◽  
Richard A. Szabo
Keyword(s):  
Gamma Globulin ◽  
Immunological Activity ◽  
Staphylococcal Enterotoxins ◽  
Double Antibody ◽  
Aggregate Fractions ◽  
Antibody Complex ◽  
Antigen Antibody

A sensitive double-antibody radioimmunoassay for staphylococcal enterotoxins A and B is described. The separation of the primary antigen–antibody complex of enterotoxin A and B was achieved with an anti-rabbit gamma globulin from goats. Radioiodinated aggregate fractions of staphylococcal enterotoxins exhibited reduced immunological activity and showed little competition with non-radioactive enterotoxin. The radioimmunoassay was successfully applied for the quantitation of enterotoxins in food.

Visualization of Antibody Transport in Rat Visceral Yolk-Sac Placenta

1982 ◽  
Vol 40 ◽  
pp. 246-247
Author(s):  
William P. Jollie
Keyword(s):  
Phosphate Buffer ◽  
Yolk Sac ◽  
Female Rats ◽  
Thin Sections ◽  
Visceral Yolk Sac ◽  
Antibody Complex ◽  
Cytochemical Reaction ◽  
Hind Foot ◽  
Antigen Antibody ◽  
Yolk Sac Placenta

A technique has been developed for visualizing antibody against horseradish peroxidase (HRP) in rat visceral yolk sac, the placental membrane across which passive immunity previously has been shown to be transferred from mother to young just prior to birth. Female rats were immunized by injecting both hind foot pads with 1 mg HRP emulsified in complete Freund's adjuvant. They were given a booster of 0.5mg HRP in 0.1 ml normal saline i.v. after one week, then bred and autopsied at selected stages of pregnancy, viz., 12, 1 7 and 22 days post coitum, receiving a second booster, injected as above, five days before autopsy. Yolk sacs were removed surgically and fixed immediately in 2% paraformaldehye, 1% glutaraldehye in 0.1 M phosphate buffer with 0.01% CaCl2 at pH 7.4, room temperature, for 3 hr, rinsed 3X in 0.1 M phosphate buffer plus 5% sucrose, then exposed to 1 mg HRP in 1 ml 0.1 M phosphate buffer at pH 7.4 for 1 hr. They were refixed in aldehydes, as above, for 1 5 min (to assure binding of antigen-antibody complex). Following buffer washes, the tissues were incubated in 3 mg diaminobenzidine tetrahydrochloride and 0.01% H2O2 in 0.05 M Tris-HCl buffer for 30 min. After brief buffer washes, they were postfixed in 2% OsO4. in phosphate buffer at pH 7.4, 4°C for 2 hr, dehydrated through a graded series of ethanols, and embedded in Durcupan. Thin sections were observed and photographed without contrast-enhancement with heavy metals. Cytochemical reaction product marked the site of HRP (i.e., antigen) which, in turn, was present only where it was bound with anti-HRP antibody.

INHIBITION OF LIPOLYTIC ACTIVITY OF SYNTHETIC β1–24 AND β1–39 CORTICOTROPHIN BY ANTI-ACTH ANTISERUM

1966 ◽  
Vol 51 (1) ◽  
pp. 88-94 ◽  
Author(s):  
A. Villanueva ◽  
S. J. H. Ashcroft ◽  
J. P. Felber
Keyword(s):  
Guinea Pig ◽  
Lipolytic Activity ◽  
Peptide Hormones ◽  
Fat Pad ◽  
Double Antibody ◽  
Epididymal Fat ◽  
Antibody Complex ◽  
Radio Immunoassay ◽  
Antigen Antibody

ABSTRACT The synthetic ACTH peptides β1–39 and β1–24 stimulated lipolysis as determined by the rat epididymal fat pad in vitro. The stimulating effect of these peptides was diminished by prior incubation of the peptides with antibodies produced by the guinea-pig against ACTH. The stimulating effect of these hormones was also diminished by the double antibody system used in the radio-immunoassay of ACTH and other peptide hormones, in which incubation with antiserum is followed by precipitation of the antigen-antibody complex by rabbit anti-guinea-pig-γ-globulin.

IDENTIFICATION OF LATS AS AN ANTIGEN-ANTIBODY COMPLEX

1973 ◽  
Vol 71 (4_Suppl) ◽  
pp. S11
Author(s):  
K. Schemmel ◽  
L. Weisbecker ◽  
H. Norden ◽  
V. Mokmol ◽  
V. Becker ◽  
...  
Keyword(s):  
Antibody Complex ◽  
Antigen Antibody

scholarly journals Recent Advances in Quenchbody, a Fluorescent Immunosensor

Sensors ◽  
2021 ◽  
Vol 21 (4) ◽  
pp. 1223
Author(s):  
Jinhua Dong ◽  
Hiroshi Ueda
Keyword(s):  
Fluorescence Intensity ◽  
Fluorescent Dyes ◽  
Antibody Fragment ◽  
Disease Diagnosis ◽  
Disease Biomarkers ◽  
Highly Sensitive ◽  
Physiologically Active Substances ◽  
New Type ◽  
Antigen Antibody ◽  
Active Substances

The detection of viruses, disease biomarkers, physiologically active substances, drugs, and chemicals is of great significance in many areas of our lives. Immunodetection technology is based on the specificity and affinity of antigen–antibody reactions. Compared with other analytical methods such as liquid chromatography coupled with mass spectrometry, which requires a large and expensive instrument, immunodetection has the advantages of simplicity and good selectivity and is thus widely used in disease diagnosis and food/environmental monitoring. Quenchbody (Q-body), a new type of fluorescent immunosensor, is an antibody fragment labeled with fluorescent dyes. When the Q-body binds to its antigen, the fluorescence intensity increases. The detection of antigens by changes in fluorescence intensity is simple, easy to operate, and highly sensitive. This review comprehensively discusses the principle, construction, application, and current progress related to Q-bodies.

scholarly journals Metabolism of Heterogenic Hemoglobins

Blood ◽  
1963 ◽  
Vol 22 (3) ◽  
pp. 334-341 ◽  
Author(s):  
RICHARD D. LEVERE ◽  
HERBERT C. LICHTMAN ◽  
Joan Levine
Keyword(s):  
Pulmonary Tuberculosis ◽  
Sickle Cell ◽  
Sickle Cell Trait ◽  
Hemoglobin S ◽  
Active Pulmonary Tuberculosis ◽  
Hemoglobin A ◽  
Abnormal Hemoglobin

Abstract The relative rates of incorporation of Fe59 into heterogenic hemoglobins was studied in four patients with sickle cell trait. Three of the patients were free of superimposed disease, while one had active pulmonary tuberculosis. In all subjects there was a significantly greater incorporation of radioiron, per milligram of hemoglobin, into hemoglobin S than into hemoglobin A. The data indicate that in sickle cell trait the rates of synthesis of the heterogenic hemoglobins are not proportional to their circulating concentrations. Two interpretations appear possible. Since the size of the intra-marrow pool of hemoglobin S was not known, it is possible that there exists a smaller preformed pool of the abnormal hemoglobin, with the isotope making its appearance first in hemoglobin S. However, it is also possible that hemoglobin S is synthesized at a rate which is greater than that reflected by its circulating concentration. This implies that the relative concentrations of hemoglobin S and hemoglobin A vary from erythrocyte to erythrocyte, and that those cells with the greatest proportion of hemoglobin S are selectively destroyed.

scholarly journals Biophysics : Aspects of Amino Acids Sequence in Proteins and Nucleotide Sequence in Nucleic Acids

2013 ◽  
Vol 4 ◽  
pp. 65-74
Author(s):  
Khadka Bahadur Chhetri
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Nucleic Acids ◽  
Polypeptide Chain ◽  
Antibody Complex ◽  
Antigen Antibody

Protein is the polypeptide chain of amino-acid sequence. Proteins of all species, from bacteria to humans, are made up from the same set of 20 standard amino acids. In order to carry out their function they must take a particular shape which is known as fold. All the enzymes hormones and antibodies are also proteins. To treat certain toxic-microorganism or invader we need certain antigen-antibody complex in the organisms. Just as amino-acid sequence forms the proteins, the polynucleotide sequence forms the nucleic acids. The gene is a part of DNA macromolecule responsible for the synthesis of protein chains. There are 20 amino-acids responsible for the formation of protein and 4 nucleotides responsible for the formation of DNA (RNA). Therefore, we can say that protein text is written in 20-letter and the DNA (RNA) text is written in 4-letter language. The information contained in genes in DNA is transferred to mRNA during transcription.The Himalayan Physics Vol. 4, No. 4, 2013 Page: 65-74 Uploaded date: 12/23/2013 

Sign in / Sign up

Export Citation Format

Share Document