The Experts below are selected from a list of 117 Experts worldwide ranked by ideXlab platform
Cai Lingfe - One of the best experts on this subject based on the ideXlab platform.
-
Application of Antiserum of Bovine Serum Albumin in Immunoprecipitation Reaction Experiment
The Journal of Medical Theory and Practice, 2005Co-Authors: Cai LingfeAbstract:Objective: To prepare Antiserum of bovine serum albumin (BSA) for obtaining high titer Antiserum. Methods: The serum of anti-BSA was prepared by immunizing rabbits with BSA. The titer of Antiserum was detected by immunoelectrophoresis and double immunodiffusion. Results: The titer of Antiserum was 1:32 in double immunodiffusion and counter immunoelectrophoresis showed a clear precipitation line in the ratio 1:16 for BSA:anti-BSA (all at 0.5g/ml BSA).Conclusion: The higher titer of Antiserum is obtained by immunizing rabbits with BSA.
Goro Eguchi - One of the best experts on this subject based on the ideXlab platform.
-
Characterization of an Antiserum against Feather Keratins of the Chick: Its Crossreaction with a Lens Protein, δ‐crystallin
Development Growth & Differentiation, 2008Co-Authors: Ryuji Kodama, Goro EguchiAbstract:We prepared an Antiserum against a fraction of solubilized keratins extracted from down feathers of newly hatched chicks. The specificity of the Antiserum was tested by double immunodiffusion, immunofluorescent staining, and immunoblotting after sodium dodecylsulfate-polyacrylamide gel electrophoresis. All the bands except “Fast protein” reacted with the Antiserum, suggesting the presence of a common antigenicity through various polypeptides in solubilized feather keratins. Delta-crystallin, which is a lens specific protein, also reacted with the Antiserum. The presence of a common antigenicity between δ-crystallin and feather and scale keratins was confirmed by affinity-purification of the Antiserum, and its significance is discussed.
Okitsugu Yamashita - One of the best experts on this subject based on the ideXlab platform.
-
Induction of non-diapause eggs by injection of anti-diapause hormone rabbit serum into the diapause type of the silkworm, Bombyx mori
Journal of Insect Physiology, 1994Co-Authors: Kunihiro Shiomi, Yuko Ishida, Motoko Ikeda, Yukihiro Sato, Hiroyuki Saito, Kunio Imai, Minoru Isobe, Okitsugu YamashitaAbstract:Abstract Polyclonal Antiserum was raised by immunizing rabbits with the synthetic diapause hormone (BomDH-I[19-Cys]) of the silkworm, Bombyx mori . By immunological analyses, the Antiserum was demonstrated to specifically recognize the diapause hormone. The Antiserum was injected into larvae, pupae and pharate adults of the Daizo strain that were destined to lay diapause eggs, to see whether the serum is able to act in vivo as an anti-hormone agent. Injection of the Antiserum at various stages from the fourth larval instar to the early pharate adult stage induced moths to lay non-diapause eggs. The effect of the Antiserum injection declined suddenly from the middle of the pharate adult stage, when diapause hormone is secreted actively. The dose-response curve demonstrated the maximal dose to be a 1.0 μl injection of the Antiserum and a half-maximal dose of 0.1 μl. When neutralized in vitro with the synthetic diapause hormone, the Antiserum lost its ability to induce non-diapause eggs, which indicates that the Antiserum inactivates diapause hormone through immunoneutralization. A transplantation experiment using suboesophageal ganglia preexposed to the Antiserum indicated that the Antiserum had no cytotoxic effects. Following injection of the Antiserum trehalase activity and glycogen content in developing ovaries were reduced to the levels found after removal of the suboesophageal ganglion. The results indicate the potential for using rabbit IgG as a simple tool for the control of neuropeptide hormone titers in insect hemolymph.
Ryuji Kodama - One of the best experts on this subject based on the ideXlab platform.
-
Characterization of an Antiserum against Feather Keratins of the Chick: Its Crossreaction with a Lens Protein, δ‐crystallin
Development Growth & Differentiation, 2008Co-Authors: Ryuji Kodama, Goro EguchiAbstract:We prepared an Antiserum against a fraction of solubilized keratins extracted from down feathers of newly hatched chicks. The specificity of the Antiserum was tested by double immunodiffusion, immunofluorescent staining, and immunoblotting after sodium dodecylsulfate-polyacrylamide gel electrophoresis. All the bands except “Fast protein” reacted with the Antiserum, suggesting the presence of a common antigenicity through various polypeptides in solubilized feather keratins. Delta-crystallin, which is a lens specific protein, also reacted with the Antiserum. The presence of a common antigenicity between δ-crystallin and feather and scale keratins was confirmed by affinity-purification of the Antiserum, and its significance is discussed.
David G. Grenache - One of the best experts on this subject based on the ideXlab platform.
-
immunofixation reveals an apparent α heavy chain caused by precipitation of fibrinogen with iga Antiserum
Clinica Chimica Acta, 2006Co-Authors: Jennifer A Snyder, Monte S. Willis, David G. GrenacheAbstract:Background Fibrinogen present in serum specimens can interfere with the interpretation of serum protein electrophoresis. We report here the unexpected precipitation of fibrinogen by an IgA Antiserum used in immunofixation electrophoresis. Methods Immunofixation electrophoresis of plasma combined with ethanol precipitation, serial dilution of plasma, and fibrinogen adsorption of the Antiserum were used to investigate the apparent immunoreactivity of a commercial source of IgA Antiserum to fibrinogen. Results Fibrinogen immunoreactivity by IgA Antiserum was observed at fibrinogen concentrations ≥ 0.93 g/l. Ethanol precipitation of plasma removed fibrinogen and prevented the immunofixation of the protein by the IgA Antiserum. Adsorption of the IgA Antiserum with human fibrinogen removed its ability to precipitate fibrinogen, demonstrating cross-reactivity between the IgA Antiserum and fibrinogen. Conclusions Commercial sources of Antiserum used for immunofixation electrophoresis may contain antibodies with specificity towards proteins typically absent from serum such as fibrinogen and can produce clinically misleading results.
-
Immunofixation reveals an apparent alpha heavy chain caused by precipitation of fibrinogen with IgA Antiserum.
Clinica chimica acta; international journal of clinical chemistry, 2006Co-Authors: Jennifer A Snyder, Monte S. Willis, David G. GrenacheAbstract:Fibrinogen present in serum specimens can interfere with the interpretation of serum protein electrophoresis. We report here the unexpected precipitation of fibrinogen by an IgA Antiserum used in immunofixation electrophoresis. Immunofixation electrophoresis of plasma combined with ethanol precipitation, serial dilution of plasma, and fibrinogen adsorption of the Antiserum were used to investigate the apparent immunoreactivity of a commercial source of IgA Antiserum to fibrinogen. Fibrinogen immunoreactivity by IgA Antiserum was observed at fibrinogen concentrations > or =0.93 g/l. Ethanol precipitation of plasma removed fibrinogen and prevented the immunofixation of the protein by the IgA Antiserum. Adsorption of the IgA Antiserum with human fibrinogen removed its ability to precipitate fibrinogen, demonstrating cross-reactivity between the IgA Antiserum and fibrinogen. Commercial sources of Antiserum used for immunofixation electrophoresis may contain antibodies with specificity towards proteins typically absent from serum such as fibrinogen and can produce clinically misleading results.