{"title":"The reduction of animal usage by the application of indirect haemagglutination in the potency testing of diphtheria toxoid in combined vaccines","authors":"S.C. Maheshwari , Suniti B. Sharma , Subhash Ahuja , S.N. Saxena","doi":"10.1016/0092-1157(88)90024-8","DOIUrl":"10.1016/0092-1157(88)90024-8","url":null,"abstract":"<div><p>Eight Adsorbed Diphtheria-Tetanus vaccines and 13 Diphtheria-Tetanus-Pertussis vaccines made by four different manufacturers were tested for the potency of the diphtheria components in guinea-pigs by the method of <span>British Pharmacopoeia (1973)</span>. Two-hundred-and-ten guinea-pig sera consisting of ten sera related to each vaccine sample thus obtained were titrated for diphtheria antitoxin by indirect haemagglutination (IHA) and the conventional toxin neutralization (TN) tests.</p><p>Statistical analysis of the results showed a good correlation between the titres obtained with the two tests. The potencies of the diphtheria components of various vaccines calculated from the antitoxin content of the respective guinea-pig sera titrated by the IHA test correlated significantly with the potencies obtained from the antitoxin content titrated by the routinely used TN test. The use of IHA in place of the TN test thus offers as an alternative that permits a reduction in animal usage.</p></div>","PeriodicalId":75991,"journal":{"name":"Journal of biological standardization","volume":"16 1","pages":"Pages 9-14"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0092-1157(88)90024-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14386526","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The purification and characterization of an acellular pertussis vaccine","authors":"M. Chazono , I. Yoshida , T. Konobe , K. Fukai","doi":"10.1016/0092-1157(88)90035-2","DOIUrl":"10.1016/0092-1157(88)90035-2","url":null,"abstract":"<div><p>An acellular pertussis vaccine manufactured by Biken<span><sup>‡</sup></span> was investigated for purity, potency and toxicity. The vaccine was composed of almost equal proportions of pertussis toxin (PT) and filamentous hemagglutinin (FHA). The purity of the vaccine was 97–99%. The protective effects of component vaccines containing various ratios of PT and FHA were tested and it was found that the ratio of 1:1 provided the most effective vaccine.</p></div>","PeriodicalId":75991,"journal":{"name":"Journal of biological standardization","volume":"16 2","pages":"Pages 83-84, IN1, 85-89"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0092-1157(88)90035-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14032009","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The development and standardization of an enzyme-linked immunosorbent assay for the detection of antibodies to bovine herpesvirus 2","authors":"Susan E. Bushnell , S. Edwards","doi":"10.1016/0092-1157(88)90028-5","DOIUrl":"10.1016/0092-1157(88)90028-5","url":null,"abstract":"<div><p>A single dilution enzyme-linked immunosorbent assay (ELISA) for the detection of antibodies to bovine herpesvirus 2 has been developed, standardized and compared with the virus neutralization test. The results of the two tests correlated well. A positive/negative threshold was established for the ELISA. The ELISA was reproducible, sensitive, rapid and specific.</p></div>","PeriodicalId":75991,"journal":{"name":"Journal of biological standardization","volume":"16 1","pages":"Pages 45-53"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0092-1157(88)90028-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13970918","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A rabies agglutination test (RAT) for rabies antibody detection","authors":"P. Perrin , P. Versmisse , P. Sureau","doi":"10.1016/0092-1157(88)90016-9","DOIUrl":"10.1016/0092-1157(88)90016-9","url":null,"abstract":"<div><p>An agglutination test has been developed for the detection of rabies antibodies aftet human vaccination. The rabies agglutination test (RAT) is based on the capability of specific antibody to agglutinate sensitized polystyrene (or latex) beads. In the RAT, latex beads were coated, in a first step, with inactivated and purified rabies virus (PV strain adapted and propagated on BHK-21 cells) and, in a second step, with bovine serum albumin. Negative control beads were coated with bovine serum albumin (BSA) only. To test for human antibody, several microliters of serum were mixed on a glass slide with an equal volume of virus-sensitized beads and the mixture was gently agitated. After a few minutes, agglutination was visible with sera which had been characterized as positive by the virus neutralization antibody (VNAb) technique. No agglutination was observed with negative sera tested with virus-coated beads or with positive sera tested with BSA-coated beads. Virus-sensitized beads were agglutinated when the virus neutralizing antibody titres were equal to or greater than 2·5 international units per ml (IU/ml) in human sera. The concordance between the RAT results and VNAb titres was about 97% when 2·5 IU/ml was taken as the cut off value for determining the positive sera with the VNAb technique. The possibility that clinicians might use the RAT as a simple means to determine sero-conversion at the end of the post-exposure treatment of patients is discussed.</p></div>","PeriodicalId":75991,"journal":{"name":"Journal of biological standardization","volume":"16 4","pages":"Pages 281-284, IN3, 285-286"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0092-1157(88)90016-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14328489","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Additives to biological substances IV—lyophilization conditions in the preparation of International Standards: An analysis by high-performance liquid chromatography of the effects of secondary desiccation","authors":"A.F. Bristow , D. Dunn , E. Tarelli","doi":"10.1016/0092-1157(88)90029-7","DOIUrl":"10.1016/0092-1157(88)90029-7","url":null,"abstract":"<div><p>Many International Standards, Reference Preparations and Reference Reagents are routinely prepared by lyophilization in the presence of ‘inert’ carriers followed by an extensive period of secondary desiccation. In this study we have used high-performance liquid chromatography (HPLC) to analyse the effects of lyophilization and secondary desiccation on initial degradation and subsequent stability of a model protein, insulin. Secondary desiccation was found to promote a reaction of the insulin with a carrier consisting of non-volatile buffer salts and a sugar. Secondary desiccation did not improve the stability of the insulin as determined by accelerated thermal degradation and analysis using the Arrhenius equation. We conclude that careful consideration needs to be given, on a case-by-case basis, to the selection of the procedures for the preparation of International Standards, particularly those ampouled in the absence of carrier proteins and intended for physicochemical analysis such as HPLC.</p></div>","PeriodicalId":75991,"journal":{"name":"Journal of biological standardization","volume":"16 1","pages":"Pages 55-61"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0092-1157(88)90029-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14408755","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Active and passive rabies immunization: The effect of administering hyperimmune globulin before the vaccine","authors":"Hans L. Bock , Larissa Milcke-Ungeheuer","doi":"10.1016/0092-1157(88)90031-5","DOIUrl":"10.1016/0092-1157(88)90031-5","url":null,"abstract":"","PeriodicalId":75991,"journal":{"name":"Journal of biological standardization","volume":"16 1","pages":"Pages 67-69"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0092-1157(88)90031-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14477783","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Oscar de Souza Lopes , Suely S.D. de Almeida Guimarães , Ricardo de Carvalho
{"title":"Studies on yellow fever vaccine III—dose response in volunteers","authors":"Oscar de Souza Lopes , Suely S.D. de Almeida Guimarães , Ricardo de Carvalho","doi":"10.1016/0092-1157(88)90034-0","DOIUrl":"10.1016/0092-1157(88)90034-0","url":null,"abstract":"<div><p>Standard and stabilized yellow fever (YF) vaccines were compared on the basis of the serological responses of human volunteers to varying doses of vaccine measured as pfu or LD<sub>50</sub>. The addition of stabilizer substances to bulk vaccine did not affect the immunogenicity and stabilized vaccine gave a consistently good performance. The vaccine fulfilled WHO recommendations in inducing 100% serological conversion in volunteers given about 200 pfu or 600 LD<sub>50</sub>.</p></div>","PeriodicalId":75991,"journal":{"name":"Journal of biological standardization","volume":"16 2","pages":"Pages 77-82"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0092-1157(88)90034-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14498138","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"IgG subclass distribution among antibodies to varicella-zoster virus in human varicella/zoster immunoglobulin preparations and the corresponding donor plasma","authors":"Kirsten Møyner , T.E. Michaelsen","doi":"10.1016/0092-1157(88)90003-0","DOIUrl":"10.1016/0092-1157(88)90003-0","url":null,"abstract":"<div><p>IgG subclasses to varicella-zoster virus (VZV) were detected in plasma from different sources used for the production of varicella/zoster immunoglobulin (VZIG). IgG1 and IgG3 were the principal virus antibodies in plasma from healthy donors as well as from convalescents after primary and reactivated disease. Anti-VZV IgG3 antibodies were predominant among varicella convalescents while IgG1 antibodies dominated among zoster convalescents. IgG4 antibodies were present in zoster convalescents and healthy donors but were rarely detected in varicella convalescents. Antiviral IgG2 antibodies were found only in a few cases. Studies of plasma samples collected from one varicella convalescent during a period of seven months following an outbreak of disease, demonstrated a rapid fall in antiviral IgG1 and IgG3, while IgG4 increased to reach a maximum six months after the onset of symptoms. The relative distribution of VZV-specific subclasses in a plasma pool was conserved during a fractionation procedure combining polyethyleneglycol 6000 precipitation with ion exchange chromatography, thus suggesting that the protective efficacy is maintained in the resulting immunoglobin preparations.</p></div>","PeriodicalId":75991,"journal":{"name":"Journal of biological standardization","volume":"16 3","pages":"Pages 157-164"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0092-1157(88)90003-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13981792","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
James Varani , Matthew J. Bendelow, William J. Hillegas
{"title":"The effect of substrate on the production of infectious virus by cells in culture","authors":"James Varani , Matthew J. Bendelow, William J. Hillegas","doi":"10.1016/0092-1157(88)90021-2","DOIUrl":"10.1016/0092-1157(88)90021-2","url":null,"abstract":"<div><p>Herpes simplex virus type I (HSV-1), infectious bovine rhinotracheitis virus (IBR) and turkey herpesvirus were examined for growth in cells cultured on three different substrates. The substrates were glass, DEAE-dextran and collagen gel. With two of the viruses, HSV-1 and IBR, there were no apparent differences in production as a function of substrate. In contrast, the amount of the turkey herpesvirus which was recovered varied greatly with the substrate. Titers were highest on glass, followed by DEAE-dextran and then collagen gel. Our previous studies have indicated that the substrate on which anchorage-dependent cells are grown <em>in vitro</em> has an affect on a number of biological and biochemical properties. The present study indicates that the production of commercially important biologicals can be affected by the substrate.</p></div>","PeriodicalId":75991,"journal":{"name":"Journal of biological standardization","volume":"16 4","pages":"Pages 333-338"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0092-1157(88)90021-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13985506","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"WHO international reference reagents for bovine and porcine proinsulins","authors":"R.E.Gaines Das , A.F. Bristow","doi":"10.1016/0092-1157(88)90006-6","DOIUrl":"10.1016/0092-1157(88)90006-6","url":null,"abstract":"<div><p>Candidate preparations for International Reference Reagents (IRR) for immunoassays of bovine and porcine proinsulin were evaluated in an international collaborative study. With the authorization of the Expert Committee on Biological Standardization of WHO, the following preparations were established as IRRs: bovine proinsulin (code 84/514, defined ampoule content 25 μg) and porcine proinsulin (84/528, 20 μg). The content of ampoules of these materials is defined in terms of mass rather than international units of activity, therefore they are IRR rather than International Standards. Both preparations are intended as primary reference reagents for the calibration of immunoassays.</p></div>","PeriodicalId":75991,"journal":{"name":"Journal of biological standardization","volume":"16 3","pages":"Pages 187-193"},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0092-1157(88)90006-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14181933","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}