scholarly journals Preparation of anti-chloramphenicol rabbit antibody

2016 ◽  
Vol 19 (4) ◽  
pp. 5-13
Author(s):  
Thinh Duc Nguyen ◽  
Thu Thi Nguyet Nguyen ◽  
Diem Ngoc Duong ◽  
Son Pham Ngoc Chu ◽  
Thuoc Linh Tran
Keyword(s):  
Rabbit Serum ◽  
Carrier Protein ◽  
Rabbit Antibody ◽  
Elisa Method ◽  
Broad Spectrum Antibiotic ◽  
Chromatography Column ◽  
The Third ◽  
Specific Affinity ◽  
Chloramphenicol Succinate ◽  
Protein Bovine Serum Albumin

Chloramphenicol (CAP) is a broad-spectrum antibiotic of high toxicity on human therefore it is being strictly controlled in food. We are interested in the development of a method of effective extraction of CAP in food based on the immunological principle using specific anti-CAP antibody combining with LC/MS/MS for the analysis of the residual CAP in food meeting the international standard. In this article, we reported experimental results on the preparation of anti-CAP rabbit antibody. Conjugative antigen between CAP and the carrier protein, bovine serum albumin, BSA (CAP-BSA) was successfully synthesized from chloramphenicol succinate and BSA with a BSA conjugating efficiency of more than 70 %, and the presence of CAP in the conjugative antigen was confirmed by ELISA method. The CAP-BSA antigen could cause good immune response in rabbit by the first antigen injection and induce the increasing production of anti-CAP antibody in rabbit serum from the third antigen injection which reached maximal value after the fifth injection. Anti-CAP antibody was purified from rabbit anti-serum in two steps: i) Removing of albumin and other non antibody proteins by 35–37 % saturated ammonium sulphate; ii) Elimination of anti-BSA antibody by the Sepharose-BSA specific affinity chromatography column. The ability of the purified anti-CAP antibody to interact and bind with CAP molecules in CAP-spiked sample was proved using a Sepharose-Anti-CAP antibody chromatography column which was made by conjugating the purified anti-CAP antibody with Sepharose beads.

scholarly journals SPECIFICITY OF ANTIBODY BOVINE ZONNA PELLUCIDAE 3 (ANTI-bZP3) TO RABBIT ZP3 BASED ON bZP3 AS CONTRACEPTIVE ANTIGENS

2010 ◽  
Vol 5 (2) ◽  
pp. 182-187
Author(s):  
Edwin Widodo ◽  
Aulanni’am Aulanni’am
Keyword(s):  
Rabbit Serum ◽  
Elisa Method ◽  
Purple Colour ◽  
Control Female ◽  
Fertilization Process ◽  
Female Rabbit ◽  
Incomplete Freund’S Adjuvant ◽  
Freund’S Adjuvant ◽  
Freund's Adjuvant ◽  
Dot Blotting

Zonna pellucidae can be develop as antigen potential candidates based on reversible immunocontraceptive vaccines. Immunogenic sites of bovine zonna pellucidae 3 (bZP3) could stimulated the presence of anti-bZP3 which be located on rabbit ZP and inhibit sperm-egg interaction on fertilization process. Purpose of this research is to detect spesific binding anti-bZP3 to rabbit oocytes using dot blotting and ELISA method. Sub cutan induction of bZP3 with Freund's adjuvant, CFA (Complete Freund's Adjuvant) for initial immunization and following by IFA (Incomplete Freund's Adjuvant) at the 14th day and 39th day. Control female rabbit injected by Tris-Cl buffer diluted in Freund's adjuvant without bZP3 antigen. Rabbit serum injected to rat for producing Rat Anti Rabbit Anti-bZP3. This research concludes spesific binding of anti-bZP3 with increasing purple colour on dot blotting methods. Anti-bZP3 increasing on 24th day and 31th day and still until 48th day. Measurement with ELISA methods showed increased titer on OD405. Highest titer showed on 31th day post immunization. Anti-bZP3 synthetized by bZP3 induced on rabbit detectable by immunohistochemistry methods on late primary oocytes, early secondary oocytes, growing secondary oocytes, and oocytes on de Graaf folicular phase. Keywords: Dot blotting, ELISA, bZP3, anti-bZP3

Incidence and mechanism of spurious increase in serum thyrotropin.

1982 ◽  
Vol 28 (3) ◽  
pp. 427-431 ◽  
Author(s):  
P J Howanitz ◽  
J H Howanitz ◽  
H V Lamberson ◽  
K M Ennis
Keyword(s):  
Human Serum ◽  
Rheumatoid Factor ◽  
Laboratory Animal ◽  
Solid Phase ◽  
Reference Interval ◽  
Rabbit Serum ◽  
Immunoradiometric Assay ◽  
Rabbit Antibody ◽  
Testing And Measurement ◽  
Animal Handlers

Abstract We previously reported spuriously high values for thyrotropin (TSH), presumably owing to an antibody in human serum that reacts with both reagent rabbit antibodies in an immunoradiometric assay (IRMA). We used this IRMA to measure TSH. Five of 20 sera from laboratory animal handlers showed spuriously high values. When we added 2 mL of nonimmune rabbit serum per liter to the labeled IRMA rabbit antibody reagent and reassayed the five affected specimens, the results were within the reference interval. Smaller additions partly corrected the TSH values, but nonimmune sera of eight other species had no effect. Substitution of goat solid-phase antibody decreased, but did not eliminate, the increases in TSH in three of the five affected sera. Chromatographic properties, results of rheumatoid factor testing, and measurement of human anti-rabbit immunoglobulin suggest that the interference is ascribable to an antibody of the IgG class that reacts with rabbit antibody. Evidently, antibody interference with IRMA procedures may be common in certain populations. It can be avoided by including nonimmune serum corresponding to the species used to produce reagent antibody.

Transferrin, the Third Carrier Protein of Folic Acid Activity in Human Serum

1972 ◽  
Vol 48 (4) ◽  
pp. 213-217 ◽  
Author(s):  
T. Markkanen ◽  
S. Virtanen ◽  
P. Himanen ◽  
R.-L Pajula
Keyword(s):  
Folic Acid ◽  
Human Serum ◽  
Carrier Protein ◽  
The Third

scholarly journals Reversed passive anaphylaxis in the guinea-pig

1940 ◽  
Vol 40 (4) ◽  
pp. 377-395 ◽  
Author(s):  
M. van den Ende
Keyword(s):  
Guinea Pig ◽  
Intravenous Injection ◽  
Guinea Pigs ◽  
Anaphylactic Shock ◽  
Cellular Mechanism ◽  
Rabbit Serum ◽  
Rabbit Antibody ◽  
Egg Albumin

Attempts to demonstrate reversed passive anaphylaxis in the guinea-pig with crystalline egg albumin as sensitizing antigen have been uniformly negative.When purified anti-pneumococcal antibody globulin was used as sensitizing antigen, reversed anaphylactic shock could be elicited in guinea-pigs by the intravenous injection of precipitins for the antibody globulin.The mild reactions which could be elicited when the total globulins from the serum of normal rabbits were used as sensitizing antigen are probably dependent on the presence of small amounts of y globulin.Reversed passive anaphylaxis, like direct anaphylaxis, is dependent on a cellular mechanism, and the success of experiments in which rabbit antibody globulin was used as sensitizing antigen depends on the acceptability of the antibody to the cells of the guinea-pig's tissues.Antigenic differences between antibody globulins and total normal globulins from rabbit serum are noted.

Value of Magnetic Resonance Spectroscopy for Diagnosis of Creatine Deficiency Syndrome

2021 ◽  
Author(s):  
Sadullah Şimşek ◽  
Salih Hattapoğlu ◽  
Faysal Ekici
Keyword(s):  
Magnetic Resonance ◽  
Magnetic Resonance Spectroscopy ◽  
Metabolic Diseases ◽  
Deficiency Syndrome ◽  
Resonance Spectroscopy ◽  
Congenital Disorders ◽  
Carrier Protein ◽  
The Third ◽  
Creatine Deficiency ◽  
Creatine Deficiency Syndrome

AbstractCreatine deficiency syndromes are congenital metabolic diseases characterized by decreased cerebral creatine levels as a result of disorders in creatine synthesis and transport. Therefore, magnetic resonance spectroscopy is a valuable tool for diagnosis. This disease can be explained by congenital disorders occurring in three forms at different stages of the creatine metabolic pathway. Two of disorders arise autosomal recessively in creatine biosynthesis, arginine-glycine amidinotransferase, and guanidinoacetate methyltransferase enzyme deficiency. The third disorder occurs as a result of an SLC6A8 variant in the form of creatine carrier protein deficiency. In this article, a patient with SLC6A8 carrier deficiency is presented.

Preparation and stability of a liquid creatine kinase isoenzyme control from rabbit serum.

1979 ◽  
Vol 25 (6) ◽  
pp. 873-876 ◽  
Author(s):  
G Lum
Keyword(s):  
Creatine Kinase ◽  
Residual Activity ◽  
Good Stability ◽  
Rabbit Serum ◽  
Hybridization Technique ◽  
Creatine Kinase Isoenzyme ◽  
The Third

Abstract The MB isoenzyme of creatine kinase (CK) may be prepared in vitro from rabbit serum containing only the MM and BB isoenzymes, by means of a hybridization technique. The MM and BB dimers dissociate in 4 mol/L urea, which allows random recombination of M and B monomers. A liquid CK-isoenzyme control can be made from mixtures of rabbit sera obtained after hybridization and stabilized with glycerol and 25 mmol of 2-mercaptoethanol per liter. A liquid control stored at 4 degrees C showed good stability over a three-month period, declining to a mean residual activity of CK of approximately 90% after three weeks and a mean residual activity of MM, MB, and BB of 80--85% after six weeks. At 25 degrees C, CK activity of the liquid control declined to 75--80% after the fourth week. CK-BB at 25 degrees C was the least stable isoenzyme, declining to 75% after the third week and reaching 60% of activity after 12 weeks. CK-MB and CK-MM showed approximately 10--15% less stability at 25 degrees C than at 4 degrees C.

scholarly journals Recombinant Group B Streptococcus Alpha-Like Protein 3 Is an Effective Immunogen and Carrier Protein

2008 ◽  
Vol 15 (7) ◽  
pp. 1035-1041 ◽  
Author(s):  
Hsiao-Hui Yang ◽  
Samantha J. Mascuch ◽  
Lawrence C. Madoff ◽  
Lawrence C. Paoletti
Keyword(s):  
Capsular Polysaccharide ◽  
Human Peripheral Blood ◽  
Rabbit Serum ◽  
Specific Response ◽  
Carrier Protein ◽  
Blood Leukocytes ◽  
C Protein ◽  
Type Iii ◽  
Group B

ABSTRACT Conjugate vaccines against pathogens of multiple serotypes are optimized when all components induce functional antibody, resulting in broadened coverage. While most clinical studies of vaccines against group B Streptococcus (GBS) have evaluated conjugates composed of capsular polysaccharide (CPS) coupled to tetanus toxoid, conjugates prepared with GBS proteins as carriers have also been efficacious in animals. Here, we report that recombinant GBS alpha-like protein 3 (rAlp3) is both a strong immunogen and a viable carrier protein for type III CPS. The type III CPS-specific immunoglobulin G (IgG) titer rose from <100 to 64,000 among mice that received type III CPS coupled to rAlp3 (III-rAlp3) compared with an absence of a specific response among mice that received an uncoupled mixture. Most (94%) newborn pups born to III-rAlp-vaccinated dams survived challenge with viable type III GBS, compared with 43% survival among those born to dams that received the uncoupled mixture (P < 0.0001). A tricomponent conjugate of type III CPS, rAlp3, and a GBS recombinant beta C protein lacking its IgA binding site (III-rAlp3-rBCPΔIgA) provided protection against a serotype III strain and a serotype Ia strain bearing beta C protein. High-titered anti-rAlp3 rabbit serum opsonized Alp3-containing strains of two GBS serotypes (types V and VIII) and invasive type III strains bearing the cross-reactive Rib protein for in vitro killing by human peripheral blood leukocytes. Thus, the potential exists for the inclusion of rAlp3 in a GBS vaccine formulated to provide multiserotype coverage.

Immunochemical properties of immunoglobulin G conjugated with lactate dehydrogenase.

1985 ◽  
Vol 31 (7) ◽  
pp. 1178-1181 ◽  
Author(s):  
K Sudo ◽  
M Maekawa ◽  
T Kanno
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Immunoglobulin G ◽  
Equilibrium Constants ◽  
Antigen Recognition ◽  
Binding Affinities ◽  
Rabbit Antibody ◽  
Human Igg ◽  
The Third ◽  
Enzyme Molecules

Abstract Quantitative binding affinities of immunoglobulin G (IgG) for the five isoenzymes of lactate dehydrogenase (LD; EC 1.1.1.27) were determined for IgG isolated from three patients' sera that contained LD-IgG complexes. These three IgGs formed soluble complexes with four (LD 1, 2, 3, 5) of the five LD isoenzymes in two of the patients and in the third they bound with three (LD 2, 3, 4) of the five LD isoenzymes without inhibiting the enzyme activity or precipitating with the enzyme molecules. When rabbit antibody to human IgG was added to these sera, the complexes between the LD isoenzymes and the patients' isolated IgG were completely precipitated. The equilibrium constants for the respective isolated IgG complexes with LD-3 were 0.102, 2.58, and 7.49 X 10(8) L/mol. In these three cases, LD-3 evoked the strongest response from the prepared IgG, demonstrating that the site of antigen recognition of LD-linked IgG was not associated with the structure of individual H and M subunits.

The absorption of antibody from immune sera and from mixtures of sera by the gut of the young rat

1958 ◽  
Vol 148 (930) ◽  
pp. 92-103 ◽  
Keyword(s):  
Marked Effect ◽  
Immune Serum ◽  
Maximum Amount ◽  
Rabbit Serum ◽  
Antibody Concentration ◽  
Globulin Fraction ◽  
Rabbit Antibody ◽  
Rat Serum ◽  
Old Rats ◽  
Immune Rabbit

The amount of antibody transmitted to the circulation from immune rat serum administered by mouth in a single dose to 12-day-old rats is directly proportional both to the antibody concentration and to the volume of serum administered for doses up to 0⋅10 ml. The amount of antibody transmitted does not increase with larger doses and is limited to that sufficient to produce a mean circulating titre of 1/32 of that of the immune serum. The uptake of the antibody-containing globulin fraction from a single feed is sufficient to account for the whole of the increase in this fraction of the young rats’ serum protein over a period of at least 9 h. The proportion of antibody transmitted to the circulation from immune rabbit serum administered by mouth declines nearly linearly with increasing volume of dose up to the maximum that could be administered of 0⋅60 ml. The proportion of rabbit antibody transmitted is approximately 1/8 of that of rat antibody from corresponding doses of immune serum up to 0⋅10 ml. Admixture of certain heterologous sera with the immune rat or rabbit serum administered by mouth interferes with the transmission of antibody to the circulation to an extent that cannot be accounted for by the dilution. Human, ox, guinea-pig and rabbit sera have a marked effect, whereas sheep, mouse, hamster and rat sera have little or no effect. Interference with the transmission of rat antibodies results even when the volume of the dose of mixed sera is less than 0⋅10 ml. Although interference decreases the proportion of antibody transmitted to the circulation it does not reduce significantly the maximum amount that can be transmitted.

scholarly journals Mitochondrial outer and inner membrane fusion requires a modified carrier protein

2009 ◽  
Vol 184 (4) ◽  
pp. 569-581 ◽  
Author(s):  
Suzanne Hoppins ◽  
Jennifer Horner ◽  
Cheng Song ◽  
J. Michael McCaffery ◽  
Jodi Nunnari
Keyword(s):  
Functional Analysis ◽  
Membrane Protein ◽  
Fusion Protein ◽  
Membrane Fusion ◽  
Outer Membrane Protein ◽  
Carrier Protein ◽  
Inner Membrane ◽  
The Third ◽  
Membrane Tethering ◽  
Related Proteins

In yeast, three proteins are essential for mitochondrial fusion. Fzo1 and Mgm1 are conserved guanosine triphosphatases that reside in the outer and inner membranes, respectively. At each membrane, these conserved proteins are required for the distinct steps of membrane tethering and lipid mixing. The third essential component is Ugo1, an outer membrane protein in the mitochondrial transport protein family. We show that Ugo1 is a modified member of this family, containing three transmembrane domains and existing as a dimer, a structure that is critical for the fusion function of Ugo1. Our functional analysis of Ugo1 indicates that it is required distinctly for both outer and inner membrane fusion after membrane tethering, indicating that it operates at the lipid-mixing step of fusion. This role is distinct from the fusion dynamin-related proteins and thus demonstrates that at each membrane, a single fusion protein is not sufficient to drive the lipid-mixing step, but instead, this step requires a more complex assembly of proteins.

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