• Korean Journal of Veterinary Research
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• v.31 no.4
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• pp.397-402
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• 1991

The present experiments were undertaken to produce the standard antiserum for equine blood typing. The following results were obtained through ISO and Hetero Immunizations of the horses whose blood typing was analysed in the Laboratory of Racing Chemistry of Japan. 1. Of the 21 combinations of ISO-immune, 17 horses were produced antibody (about 80%) 2. Antibody titers were increased from early 1 week to late 5 weeks and any antibody titers were not be obtained in spite of the using of adjuvant and 10 repeated injections in the other 4 horses. 3. High antibody titers were obtained within the earliest period in the Dd antigen but were not increased over 32 times in spite of 8~10 repeated injections in the antigen. 4. Antibody were easily produced in the Ca antigen of ISO-Immune but production of antisera were tailed due to abscence of absorbed blood cell. 5. Antibody titers of 1,024 times were obtained through 5 injections in the Ca of HeteroImmune 6. Of the produced 15 antisera (16 system), 13 antigen (5 system) were absorbed.

• Journal of Plant Biology
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• v.28 no.3
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• pp.207-216
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• 1985

Radial immunodiffusion, rocket immunoelectrophoresis, and Boyden procedure have been employed as quantitative analysis of pollen proteins in a systematic investigation of selected amentiferous plant taxa. Data presented here are continued and supplementary to the previous qualitative analysis of immunoprecipitin systems for the same purpose. Although the number of taxa tested has been limited, the serological evidence indicates that the Betulaceae has the greatest similarity to the Fagaceae, next to the Juglandaceae, the least to the Salicaceae, when antisera against Alnus hirsuta and Betula platyphylla var. japonica were used for tests. Within the Betulaceae Alnus and Betula show greatly similar affinities together, but less similar to the rest of genera: Carpinus, Carya and Corylus. When antisera against Quercus aliena, Q. dentata, and Q. glauca were used for tests, the following decreasing order to serological affinities was obtained: Quercus Alnus, Betula Carpinus, Carya, Corylus Juglans, Pterocarya Populus. Overall serological data come closer to supportint the classification systems of Cronquist, Takhtajan, and Hutchinson; but less of Thorne and Bessey. In addition this investigation indicated that pollen, with its high protein content, provided an excellent source of extractable antigens for serosystematic researches.

• Archives of Pharmacal Research
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• v.17 no.5
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• pp.318-322
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• 1994

Upon gel filtration, the commercial bovine milk xanthine oxidase preparation was fractionated into two preparations showing enzyme activity. Native polyacrylamide gel electrophoresis showed that one was in a dimeric form and the other was a monomer having molecular weight of 150 kDa. It was also found that this commercial enzyme existed mostly in an active monomeric form without loss of enzyme activity. The rabbit antisera produced against two enzyme preparations cross-reacted well each other. In SDS-polyacrylamide gtel electro-phoresis, however, both enzyme preparations yielded two smaller protein bands below 150 kDa, which appeared to bind with both antisera with high affinity but not to retain enzyme activity. It implies that bovine milk xanthine oxidase can lose its activity when monomeric subunit is further degraded.

• Journal of Oral Medicine and Pain
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• v.24 no.3
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• pp.261-267
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• 1999

The present investigation was carried out to identify salivary components of mucosal pellicle and to explore the difference of mucosal pellicle components according to the location of oral mucosa. By using antisera and immunoblotting, high-(MG1) and low-(MG2) molecular-mass salivary mucins, amylase, IgA, proline-rich proteins(PRPs) were detected in mucosal pellicle in vivo. In addition, the data indicated that mucins, IgA and proline-rich proteins could be cleaved into lower-molecular-mass products, whereas the IgA, proline-rich proteins could also be cross-linked into higher-molecular-mass complexes. Mucosal pellicles from buccal, labial and palatal mucosa showed similar pattern in immunoblotting experiments using anti-MG2 and anti-PRPs antisera. The data from this study suggest that during mucosal pellicle formation multiple components of saliva adsorb to oral mucosal epithelial cell surfaces, and selected components can be proteolytically cleaved into smaller fragments and/or cross-linked into higher-molecular products.

• The Journal of the Korean Society for Microbiology
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• v.18 no.1
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• pp.67-71
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• 1983

Antisera to ox red blood cells were prepared by injection of ox red blood cell stroma without adjuvant in outbred white rabbits. Purified IgM fraction for T-cell subset assay was obtained from these rabbit anti-ox red blood cell stroma antisera by precipitation with 50% saturated ammonium sulphate followed by DEAE-Cellulose chromatography and Sephadex G-200 gel filtration. The serological identification of purified IgM fraction was achieved by immunoelectrophoresis with guinea pig antiserum against rabbit anti-ox red blood cell IgM antibody.

• Journal of fish pathology
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• v.28 no.1
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• pp.9-15
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• 2015

The potential of Streptococcus iniae glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as an antigen for a subunit vaccine was investigated using a zebrafish model. The recombinant S. iniae GAPDH was purified using His-tag column chromatography, and antisera against the recombinant GAPDH (rGAPDH) were produced by intraperitoneal immunization of rats. By immunization with S. iniae rGAPDH, the survival rates of zebrafish against an S. iniae challenge increased, suggesting that GAPDH would be an antigen capable of inducing protective immune responses in fish. Furthermore, we demonstrated using Western blotting, that the antisera against rGAPDH of S. iniae had cross-reactivity with GAPDH from Streptococcus parauberis and Lactococcus garviae, which are also culprits of streptococcosis in cultured fish in Korea. These results suggest that S. iniae GAPDH may be used as an antigen for the development of a subunit vaccine against streptococcosis caused by diverse cocci in cultured fish.

• 대한핵의학회:학술대회논문집
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• 1980.05a
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• pp.3.2-4
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• 1980

• Journal of fish pathology
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• v.3 no.1
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• pp.11-19
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• 1990

Yellow tail (Seriola quinqueradiata) infected by Pasteurella piscicida have been occurred to mass mortality without showing apparent surface lesions in cage culture farms. In this case, it is necessary to consider countermeasure by rapid diagnosis of infected fish. The purpose of the present study was to investigate usefulness of the direct fluorescent antibody technique(FAT) for rapid diagnosis of pseudotuberclosis of cultured yellowtail caused by P. piscicida. Antibody produced by inoculating rabbit with formalin killed pseudotuberclosis bacteria antigen(strain KNP-2). Immunoglobulin-G(IgG) was purified from antisera by DEAE-cellulose column chromatography and conjugate with fluorescein isothiocyanate. Fluorescein-labeled antisera was purified by sephadex G-25 gel column chromatography. The fluorescein/protein molar ratio of labeled antisera was determined as 8.8-9.5. Diagnosis of cultured yellowtail was examined in cage culture farms which located in Tongyung, kyungnam from July to October 1990. The causative bacteria of pseudotuberclosis could be detected within two hours after the specimens were transferred to the laboratory for FAT, and it showed that FAT could be adapted as a rapid and accurate diagnostic method of pseudotuberclosis in yellowtail.

• Journal of Microbiology and Biotechnology
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• v.7 no.6
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• pp.423-428
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• 1997

Vibrio vulnificus is a halophilic gram-negative human pathogen, which affects people with underlying liver diseases or a suppressed immune system, often leading to primary septicemia with a mortality rate of higher than 60%. In an effort to develop an oral vaccine against V. vulnificus infection, we prepared a whole cell killed vaccine of V. vulnificus on a large scale and compared the immunogenicity and protective efficacy of the vaccine administered in three formulation forms in rabbits. Since V. vulnificus O-antigen serotypes 1, 2, 3, 4, 5, and 7 account for more than 95% of clinical isolates, we prepared cell lysates from these six serotype strains and mixed in equal amounts for a vaccine. The vaccine was administered to rabbits intramuscularly (i.m.), orally as granules or as enteric-coated granules. In rabbits, all three formulation forms elicited a high level of serum IgG antibody reactive not only to the six strains but also to other O-antigen serotypes 6, 8 and 9, indicating cross-reactivities among the strains. Immunotherapeutic efficacy of the antisera was also evaluated by a passive immunization assay, which revealed that the orally immunized antisera as well as the i.m. immunized antisera was protective against a subsequent lethal challenge of V. vulnificus. These data demonstrate that oral immunization with a V. vulnificus whole cell lysate vaccine induced a systemic immune response and suggest the feasibility of development of this vaccine preparation as an oral vaccine.

• International Journal of Industrial Entomology and Biomaterials
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• v.2 no.1
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• pp.55-59
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• 2001

The vitellin of the red flour beetled Tribolium castaneum Herbst was purified and characterized. The vitellin of T. castaneum was purified by the FPLC techniques, anion exchange chromatography and gel permeation chromatography. In native-polyacrylamide gel electrophoresis, vitellin of T. castaneum was detected as a single band. This native vitellin has molecular weight of 440 kDa. The vitellin of T. castaneum is composed of three polypeptides, designated Vnl (178 kDa), Vn2 (168 kDa) and Vn3 (52 kDa) in SDS-polyacrylamide gel electrophoresis. Three subunits of vitellin were presented in the female adult hemolymph and egg extracts, but not observed in the male. These three polypeptides gradually decreased during embryogenesis. Polyclonal antiserum raised against purified vitellin reacted with the three polypeptides, Vnl, Vn2 and Vn3. Antisera raised against Vn1 and Vn2 cross-reacted with the two large subunits, Vnl and Vn2, respectively. Another subunits Vn3, however, was not cross-reacted with these two antisera. Also, antiserum raised against Vn3 did not cross-react with the Vn1 and Vn2.