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| 6-aminopenicillanic acid |
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| CHEBI:16705 |
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| A penicillanic acid compound having a (6R)-amino substituent. The active nucleus common to all penicillins, it may be substituted at the 6-amino position to form the semisynthetic penicillins, resulting in a variety of antibacterial and pharmacologic characteristics. |
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This entity has been manually annotated by the ChEBI Team.
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CHEBI:20705, CHEBI:2172
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| ZINC000008216134 |
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Molfile
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SDF
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more structures >>
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| 6-APA ((+)-6-aminopenicillanic acid) is an organic compound that is used in the synthesis of β–lactam antibiotics including amoxicillin, ampicillin, oxacillin, and carbenicillin. The major commercial source of 6-APA is natural penicillin G, which contains an N-phenylacetyl substituent.
The semi-synthetic penicillins derived from 6-APA are also referred to as penicillins and are considered part of the penicillin family of antibiotics.
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Read full article at Wikipedia
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InChI=1S/C8H12N2O3S/c1- 8(2)4(7(12)13)10-5(11)3(9)6(10)14-8/h3-4,6H,9H2,1-2H3,(H,12,13)/t3-,4+,6-/m1/s1 |
| NGHVIOIJCVXTGV-ALEPSDHESA-N |
| C([C@H]1C(S[C@@]2([C@@H](C(N12)=O)N)[H])(C)C)(O)=O |
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Bronsted acid
A molecular entity capable of donating a hydron to an acceptor (Bronsted base).
(via oxoacid )
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allergen
A chemical compound, or part thereof, which causes the onset of an allergic reaction by interacting with any of the molecular pathways involved in an allergy.
antimicrobial agent
A substance that kills or slows the growth of microorganisms, including bacteria, viruses, fungi and protozoans.
(via heterocyclic antibiotic )
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View more via ChEBI Ontology
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6-amino-2,2-dimethylpenam-3α-carboxylic acid
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(+)-6-aminopenicillanic acid
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ChEBI
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(2S,5R,6R)-6-amino-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylic acid
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IUPAC
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6-Aminopenicillamine acid
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ChemIDplus
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6-Aminopenicillanate
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KEGG COMPOUND
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6-Aminopenicillanic acid
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KEGG COMPOUND
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6-APA
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ChEBI
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6-Apa
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ChemIDplus
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6-Aps
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ChemIDplus
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6β-aminopenicillanic acid
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ChEBI
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Aminopenicillanic acid
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ChemIDplus
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Penicin
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ChemIDplus
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Penin
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ChemIDplus
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Phenacyl 6-aminopenicillinate
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ChemIDplus
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15080
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Reaxys Registry Number
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Reaxys
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1876702
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Gmelin Registry Number
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Gmelin
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551-16-6
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CAS Registry Number
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KEGG COMPOUND
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551-16-6
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CAS Registry Number
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ChemIDplus
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959078
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Beilstein Registry Number
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Beilstein
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Avinash VS, Chauhan PD, Gaikwad S, Pundle A (2017)
Biotransformation of penicillin V to 6-aminopenicillanic acid using immobilized whole cells of E. coli expressing a highly active penicillin V acylase.
Preparative biochemistry & biotechnology 47, 52-57 [PubMed:26986755]
[show Abstract]
The production of 6-aminopenicillanic acid (6-APA) is a key step in the manufacture of semisynthetic antibiotics in the pharmaceutical industry. The penicillin G acylase from Escherichia coli has long been utilized for this purpose. However, the use of penicillin V acylases (PVA) presents some advantages including better stability and higher conversion rates. The industrial application of PVAs has so far been limited due to the nonavailability of suitable bacterial strains and cost issues. In this study, whole-cell immobilization of a recombinant PVA enzyme from Pectobacterium atrosepticum expressed in E. coli was performed. Membrane permeabilization with detergent was used to enhance the cell-bound PVA activity, and the cells were encapsulated in calcium alginate beads and cross-linked with glutaraldehyde. Optimization of parameters for the biotransformation by immobilized cells showed that full conversion of pen V to 6-APA could be achieved within 1 hr at pH 5.0 and 35°C, till 4% (w/v) concentration of the substrate. The beads could be stored for 28 days at 4°C with minimal loss in activity and were reusable up to 10 cycles with 1-hr hardening in CaCl2 between each cycle. The high enzyme productivity of the PVA enzyme system makes a promising case for its application for 6-APA production in the industry. | Su M, Sun H, Zhao Y, Lu A, Cao X, Wang J (2016)
Degradation Kinetics and Mechanism of a β-Lactam Antibiotic Intermediate, 6-Aminopenicillanic Acid, in a New Integrated Production Process.
Journal of pharmaceutical sciences 105, 139-146 [PubMed:26852849]
[show Abstract]
In an effort to promote sustainability and to reduce manufacturing costs, the traditional production process for 6-aminopenicillanic acid (6-APA) has been modified to include less processing units. The objectives of this study are to investigate the degradation kinetics of 6-APA, to propose a reasonable degradation mechanism, and to optimize the manufacturing conditions within this new process. A series of degradation kinetic studies were conducted in the presence of impurities, as well as at various chemical and physical conditions. The concentrations of 6-APA were determined by high-performance liquid chromatography. An Arrhenius-type kinetic model was established to give a more accurate prediction on the degradation rates of 6-APA. A hydrolysis degradation mechanism is shown to be the major pathway for 6-APA. The degradation mechanisms and the kinetic models for 6-APA in the new system enable the design of a good manufacturing process with optimized parameters. | Balci H, Ozturk MT, Pijning T, Ozturk SI, Gumusel F (2014)
Improved activity and pH stability of E. coli ATCC 11105 penicillin acylase by error-prone PCR.
Applied microbiology and biotechnology 98, 4467-4477 [PubMed:24389703]
[show Abstract]
Penicillin G acylase is the key enzyme used in the industrial production of β-lactam antibiotics. This enzyme hydrolyzes penicillin G and related β-lactam antibiotics releasing 6-aminopenicillanic acid, which is an intermediate in the production of semisynthetic penicillins. To improve the enzymatic activity of Escherichia coli penicillin acylase, sequential rounds of error-prone polymerase chain reaction were applied to the E. coli pac gene. After the second round of evolution, the best mutant M2234 with enhanced activity was selected and analyzed. DNA sequence analyses of M2234 revealed that one amino acid residue (K297I), located far from the center of the catalytic pocket, was changed. This mutant (M2234) has a specific activity 4.0 times higher than the parent enzyme and also displayed higher stability at pH 10. | Demirci S, Demirbas A, Ulker S, Alpay-Karaoglu S, Demirbas N (2014)
Synthesis of some heterofunctionalized penicillanic acid derivatives and investigation of their biological activities.
Archiv der Pharmazie 347, 200-220 [PubMed:24293403]
[show Abstract]
6-Substituted amino-penicillanic acid esters were synthesized starting with 6-apa. The compounds containing a 1,3-thiazole- or 1,3-thiazolidinone nucleus linked to the penicillanic acid skeleton via a hydrazino linkage were obtained from 6-apa. The treatment of carbonylamino and carbonothioylamino compounds with 4-chlorophenacyl bromide or ethyl bromoacetate gave 6-bis{4-[1,3-thiazol(idinone)amino]benzoyl}amino derivatives of 6-apa. Benzyl derivatives were synthesized in several steps, starting with 4-aminobenzoyl chloride. The treatment of 4-{[3-benzyl-4-oxo-1,3-thia(oxa)zolidin-2-ylidene]amino}benzoyl chlorides with 6-apa in ethanolic solution produced the 6-[bis(4-{[3-benzyl-4-oxo-1,3-thiazolidin-2-ylidene]amino}benzoyl)amino] derivative of penicillanic acid, while the reaction of the same intermediates in DMF gave the mono-substituted amino derivative of 6-apa. The synthesized compounds were screened for their biological activities, and some of them were found to possess good to moderate antimicrobial activity. Moreover, some of the compounds displayed antiurease, anti-β-lactamase, and/or antilipase activities. | Nandi A, Pan S, Potumarthi R, Danquah MK, Sarethy IP (2014)
A Proposal for Six Sigma Integration for Large-Scale Production of Penicillin G and Subsequent Conversion to 6-APA.
Journal of analytical methods in chemistry 2014, 413616 [PubMed:25057428]
[show Abstract]
Six Sigma methodology has been successfully applied to daily operations by several leading global private firms including GE and Motorola, to leverage their net profits. Comparatively, limited studies have been conducted to find out whether this highly successful methodology can be applied to research and development (R&D). In the current study, we have reviewed and proposed a process for a probable integration of Six Sigma methodology to large-scale production of Penicillin G and its subsequent conversion to 6-aminopenicillanic acid (6-APA). It is anticipated that the important aspects of quality control and quality assurance will highly benefit from the integration of Six Sigma methodology in mass production of Penicillin G and/or its conversion to 6-APA. | Ariza A, Barrionuevo E, Mayorga C, Montañez MI, Perez-Inestrosa E, Ruiz-Sánchez A, Rodríguez-Guéant RM, Fernández TD, Guéant JL, Torres MJ, Blanca M (2014)
IgE to penicillins with different specificities can be identified by a multiepitope macromolecule: Bihaptenic penicillin structures and IgE specificities.
Journal of immunological methods 406, 43-50 [PubMed:24631718]
[show Abstract]
Quantitation of specific IgE by immunoassay is a recommended in vitro test for the diagnosis of immediate hypersensitivity reactions to betalactams (BLs), particularly when skin test results are negative. IgE antibodies that recognize the common nuclear structure of all BLs or the specific side chain structure can be mainly distinguished by immunoassays. The aim of this study was to develop an immunoassay system to detect IgE antibodies with different specificities. Cellulose discs conjugated with benzylpenicillin (BP), amoxicillin (AX) or both drugs, with poly-l-lysine (PLL) as carrier molecule, were used as solid phases in the radioallergosorbent test (RAST). Direct and inhibition radioimmunoassay studies were made to verify the structures recognized by serum IgE antibodies from penicillin-allergic patients. Our results indicated that the addition of both haptens did not decrease the capacity to capture IgE when serum specific to either BP or AX was used, at least in terms of sensitivity. In addition, the inclusion of two haptens improved significantly the levels of IgE detection in patients who recognized both BP and AX. Therefore, the use of a solid phase with a carrier molecule conjugated with two determinants (AX and BP) is helpful to recognize IgE antibodies against either of these determinants and is useful for screening sera with different specificities. | Dolui AK, Das S (2011)
Comparative study of 6-APA production by free and agar immobilized bacteria in nutrient broth culture.
Indian journal of experimental biology 49, 289-292 [PubMed:21614893]
[show Abstract]
In the present study different bacterial samples were isolated from soil of different places of Dibrugarh and screened for biotransformation ability to produce 6-Aminopenicillanic acid. Among ten isolated bacterial samples, three gram positive bacterial samples designated as AKDD-2, AKDD-4 and AKDD-6 showed the production of 6-APA from penicillin G. Assessment of production of 6-APA after incubation in penicillin G (2 mg/ml) by three different samples separately in free and agar immobilization state was done by HPLC analysis. Reusability of immobilized cells was found successful up to 14 days. | Chen Z, Wang H, Chen Z, Ren N, Wang A, Shi Y, Li X (2011)
Performance and model of a full-scale up-flow anaerobic sludge blanket (UASB) to treat the pharmaceutical wastewater containing 6-APA and amoxicillin.
Journal of hazardous materials 185, 905-913 [PubMed:20970923]
[show Abstract]
A full-scale test was conducted with an up-flow anaerobic sludge blanket (UASB) pre-treating pharmaceutical wastewater containing 6-aminopenicillanic acid (6-APA) and amoxicillin. The aim of the study is to investigate the performance of UASB in the condition of a high chemical oxygen demand (COD) loading rate from 12.57 to 21.02 kgm(-3)d(-1) and a wide pH from 5.57 to 8.26, in order to provide a reference for treating the similar chemical synthetic pharmaceutical wastewater containing 6-APA and amoxicillin. The results demonstrated that the UASB average percentage reduction in COD, 6-APA and amoxicillin were 52.2%, 26.3% and 21.6%, respectively. In addition, three models, built on the back propagation neural network (BPNN) theory and linear regression techniques were developed for the simulation of the UASB system performance in the biodegradation of pharmaceutical wastewater containing 6-APA and amoxicillin. The average error of COD, 6-APA and amoxicillin were -0.63%, 2.19% and 5.40%, respectively. The results indicated that these models built on the BPNN theory were well-fitted to the detected data, and were able to simulate and predict the removal of COD, 6-APA and amoxicillin by UASB. | Zhao Y, Qiao H (2003)
Detection of specific IgE antibodies to major and minor antigenic determinants in sera of penicillin allergic patients.
Chinese medical journal 116, 1904-1910 [PubMed:14687482]
[show Abstract]
ObjectiveTo investigate the mechanism(s) of penicillins allergic reaction.MethodsThe radioallergosorbent test (RAST) was used to detect 9 specific IgE antibodies, including major antigenic determinants: benzylpenicilloyl (BPO), ampicilloyl (APO), amoxicilloyl (AXO), phenoxomethylpenicilloyl (PVO) and flucloxacilloyl (FLUO), and minor antigenic determinants: benzylpenicillanyl (BPA), amoxicillanyl (AXA), 6-aminopenicillanic (APA) and phenoxomethylpenicillany (PVA), in the sera of 32 penicillin allergic patients. The relationship between specific IgE antibodies and penicillins chemical structures was studied by radioallergosorbent inhibition test.ResultsNineteen of 32 patients (59.4%) were RAST positive, among whom, five cases were positive only to one or two antigenic minor determinants, and three cases were positive only to one or three major antigenic determinants. The remaining 11 patients were positive not only to major antigenic determinants but also minor antigenic determinants. In 9 specific IgE antibodies, the positive rate of PVA-IgE was the highest (34.38%), followed by BPO-IgE (31.25%). The positive rate of FLUO-IgE was the lowest (15.63%). Of the total patient group, 53.13% were positive to one or more minor antigenic determinants, while 37.5% (12/32) were positive to one or more major antigenic determinants. The percentage of patients with urticarial reactions who were positive to minor antigenic determinants (63.16%) was significantly higher than observed in the anaphylactic shock group (38.5%, P < 0.05).ConclusionsThe minor antigenic determinant was important in allergic reaction. The combining sites of the specific IgE antibodies were likely to be the side-chain of drug or the overwhelming drug molecule. | Zhao Z, Baldo BA, Rimmer J (2002)
beta-Lactam allergenic determinants: fine structural recognition of a cross-reacting determinant on benzylpenicillin and cephalothin.
Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology 32, 1644-1650 [PubMed:12569987]
[show Abstract]
BackgroundAn appreciation of the structural heterogeneity of allergenic determinants on penicillins and cephalosporins reveals the importance of side-chain groups and their involvement in many allergies to beta-lactam drugs. Although allergenic cross-reactions between penicillins and cephalosporins are known to occur, the precise molecular bases of such recognitions and cross-sensitivities have rarely been studied and identified.ObjectivesThe unexpected finding of a high incidence of positive IgE antibody reactions with both benzylpenicillin and cephalothin prompted serological and immunochemical studies to identify the chemical basis of antibody recognition of these drugs from the two different families of beta-lactam antibiotics.MethodsAdsorption studies were employed to identify whether or not a single population of antibodies was involved in the recognition of benzylpenicillin and cephalothin. Identification of the fine structural features recognized by IgE antibodies was investigated by quantitative hapten inhibition studies employing carefully selected beta-lactam drugs, analogues and some other structurally related chemicals.ResultsAdsorption studies with penicilloic acid-solid phase clearly established that a single population of cross-reacting antibodies recognized both benzylpenicillin and cephalothin. Quantitative inhibition findings, especially with phenylacetic acid and 2-thiopheneacetic acid and with cephaloridine and cefoxitin, which have the same (2-thienyl)methyl side-chain as cephalothin, implicated the methylene group as the focus of the allergenic determinant recognized on benzylpenicillin and cephalothin. In addition to the methylene group, recognition graded into neighbouring structures including the amide group and extended weakly to the beta-lactam ring.ConclusionsResults confirmed that structural features as small as a methylene group may be allergenically important. In the present case, this group, making up only part of the different side-chains on benzylpenicillin and cephalothin, together with neighbouring structures extending toward the beta-lactam ring, accounted for the cross-reactivity seen between structures that, at first sight, appear to be not closely related. Such subtle, small, common structural features are likely to be immunologically recognized and implicated in allergic reactions to other drugs, including beta-lactam antibiotics. | Shimizu T, Souma S, Nagakura N, Masuzawa T, Iwamoto Y, Yanagihara Y (1992)
Epitope analysis of aztreonam by antiaztreonam monoclonal antibodies and possible consequences in beta-lactams hypersensitivity.
International archives of allergy and immunology 98, 392-397 [PubMed:1384868]
[show Abstract]
Three cell lines producing monoclonal antibodies, Az-1 (IgG1), Az-2 (IgG1) and Az-3 (IgM) against aztreonam were established. The epitopes and the cross-reactions of the antibodies with various beta-lactams, which were conjugated with human serum albumin (HSA), were examined by enzyme-linked immunosorbent assay (ELISA) and ELISA inhibition test. In ELISA, Az-1 and Az-2 reacted only with aztreonam and ceftazidime, which have the same acyl side chain. Furthermore, Az-2 showed a strong cross-reaction with carumonam. In the ELISA inhibition test, Az-1 and Az-2 were inhibited from binding to aztreonam-HSA by aztreonam, ceftazidime, aztreonam hydrolysate, aztreonam-epsilon-amino-n-caproic acid (EACA) and ceftazidime-EACA. Az-2 was also inhibited with carumonam. From the above results, it seems that Az-1 can recognize only the degraded structure of monobactam nucleus, and Az-2 can recognize the degraded nucleus moiety and the acyl side chain. On the other hand, Az-3 displayed broad cross-reaction to various beta-lactams in ELISA. Furthermore, the MAb showed no inhibitory reaction with various beta-lactams except aztreonam- and ceftazidime-EACA conjugates in the ELISA inhibition test, suggesting that Az-3 recognize a new antigenic determinant (NAD), which is formed by the conjugation of beta-lactam and carrier protein. The above results indicate that antibodies can recognize at least three epitopes of the degraded product(s) of aztreonam nucleus, acyl side chain and NAD in aztreonam-protein conjugate. | Harle DG, Baldo BA (1990)
Identification of penicillin allergenic determinants that bind IgE antibodies in the sera of subjects with penicillin allergy.
Molecular immunology 27, 1063-1071 [PubMed:1701026]
[show Abstract]
Much of the literature on penicillin hypersensitivity is devoted to the identification of penicillin antigens rather than allergens. Human IgE-binding determinants on different penicillins have rarely been closely investigated with the view of defining fine structural allergenic features and differences. We have developed radioimmunoassays employing ampicillin, amoxicillin and ticarcillin solid phases for the detection of penicillin-reactive IgE antibodies. Quantitative hapten inhibition studies employed to identify IgE-binding regions on the penicillin molecules revealed a heterogeneous group of allergenic determinants consisting exclusively, or in part, of the alpha-aminobenzyl and benzyl side chain groups and the beta-lactam and thiazolidine rings of the penicillin nucleus. | Shiho O, Nakagawa Y, Tsuchiya K (1981)
IgE antibodies for penicillins and cephalosporins in rats. II. Antigenic specificity of rat anti-penicillin-OvA IgE sera.
The Journal of antibiotics 34, 79-83 [PubMed:6166603]
[show Abstract]
Sprague Dawley (SD) rats were immunized with various penicillin-ovalbumin (OvA) in combination with aluminum hydroxide (alum) and thimerosal-killed Bordetella pertussis for the purpose of obtaining rat anti-penicillin IgE sera. In the rat 60-hour passive cutaneous anaphylaxis (PCA) reaction and the hapten inhibition test, a weak cross reaction between penicillin G (PCG) and ampicillin (ABPC) was observed, but not cross reaction was observed between sulbenicillin (SBPC) and other penicillins. Rat anti-6-formamidopenicillanic acid (FPC) IgE serum reacted with PCG-bovine gamma globulin (BGG), ABPC-BGG and SBPC-BGG, but FPC-BGG did not react with rat anti-PCG, anti-ABPC and anti-SBPR IgE sera and the PCA reaction between anti-FPC IgE sera and FPC-BGG was inhibited by FPC, PCG, ABPC and SBPC. These results indicate that the antigenic active sites of PCG, ABPC and SBPC are limited to the acyl side chain moiety of penicillins, while the antigenic active site of FPC is confined to the penicilloyl moiety of the penicillin. |
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