2005
DOI: 10.5483/bmbrep.2005.38.1.071
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Production and Characterization of Monoclonal Antibodies against Human Ceruloplasmin

Abstract: Ceruloplasmin (CP) is the major plasma antioxidant and copper transport protein. Monoclonal antibodies (mAbs) against human CP were produced and characterized. A total of five hybridoma cell lines were established (CP2, CP10, CP20, CP25, CP30). From the epitope mapping analysis, two subgroups of mAbs recognize different peptide fragments were identified. When the purified CP was incubated with the mAbs, the ferroxidase activity of CP was inhibited up to a maximum 57 %. Immunoblotting with various tissue homoge… Show more

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Cited by 1 publication
(2 citation statements)
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“…Production of Monoclonal Antibody for HP Q8CHP8. The production of a monoclonal antibody against HP Q8CHP8 was performed as previously described. , Briefly, the purified enzyme was mixed with an equal volume of complete Freund's adjuvant and was injected intraperitoneally into a BALB/c mouse (6−8 weeks old). Two booster injections with incomplete Freund's adjuvant at 3-week intervals were followed by a final injection without adjuvant at 3 days before the cell fusion experiment.…”
Section: Methodsmentioning
confidence: 99%
See 1 more Smart Citation
“…Production of Monoclonal Antibody for HP Q8CHP8. The production of a monoclonal antibody against HP Q8CHP8 was performed as previously described. , Briefly, the purified enzyme was mixed with an equal volume of complete Freund's adjuvant and was injected intraperitoneally into a BALB/c mouse (6−8 weeks old). Two booster injections with incomplete Freund's adjuvant at 3-week intervals were followed by a final injection without adjuvant at 3 days before the cell fusion experiment.…”
Section: Methodsmentioning
confidence: 99%
“…The HAD superfamily was discovered by computer analysis of bacterial HADs, 32 catalyzing the cleavage of substrate C-Cl, P-C, and P-OP bonds via nucleophilic substitution pathways and typically showing low sequence identity <15% to family members. 33 All sequence alignment searches showed low sequence identity (22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34)(35)(36)(37)(38)(39)(40).8%) of HP Q9CXN1 to HAD superfamily members ( Table 2). HAD superfamily catalytic sites forming the so-called "core" domain 32 in HP Q9CXN1 with typical conserved amino acids is shown in Figure 5: motif I (sequence position 8-17, AVLVDLNGTL) with conserved aspartate, motif II (sequence position 41-45, VRFVT) with a conserved arginine for phosphate binding, and motif III (sequence position 182-208, KTFFLEALRDADCAPEEAVMIGDDCRD) with conserved carboxylate residues for metal binding ( Figure 5).…”
Section: Identification Of Hps In Mouse Hippocampusmentioning
confidence: 98%