Interaction of Starfish Embryonic Cells with the Complex of Okadaic Acid and Monoclonal Antibody Specific to Okadaic Acid

Ikegami, Susumu; Shimizu, Takahiko; Kajiyama, Noboru; Usagawa, Takashi; Uemura, Daisuke; Uda, Takaaki

doi:10.1271/bbb.56.1666

Cited by 2 publications

(1 citation statement)

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“…The authors also reported that OA spiroketal I, which lacks the F-and G-rings of OA, inhibits serologic binding -60 times less effectively and therefore, the F-and G-rings of OA may comprise part of the epitopes recognized by some of the polyclonal antibodies. Ikegami et al (1992) developed monoclonal antibody (OA-3) against ovalbumin-conjugated OA and reported that the antibody belongs to the IgG class with a kappa chain.…”

Section: Discussionmentioning

confidence: 99%

Elisa for Detecting Okadaic Aced in Model Systems Using Purified Polyclonal Antibodies

Dixon

Hamdy

Hayden

et al. 1997

Rapid Methods Automation Mic

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Polyclonal antibodies were produced in rabbits against okadaic acid (OA) following its coupling to bovine serum albumin using standard carbodiimide condensation procedure to form the immunogen. The immunogen was dialyzed against Tris buffer pH 7.45 at 4C and used to immunize two rabbits. Each rabbit received (at four sites) 0.5 mL. immunogen (id.) together with adjuvant followed by three repeated injections of 0.3 mL. ernulsijied immunogen-adjuvant mixture at weekly intervals. The last injection was made 60 days after the fourth. The antiserum was collected, at intervals, the immunoglobulin fraction (Ig G) isolated, purified and used in an ELISA system to capture the okadaic moiety of the immunogen. Antibody titers increased following repeated immunization and the IgG recognized low levels of OA. However, ELISA was more sensitive for detecting the immunogen than for pure OA, but using the biotinylated-IgG enhanced the titration to both and the detection limit for OA was 0.63 ng per 0. I mL buffer-methanol and the assay linearity rangedfrom 0.63 to 5.0 ng OA.

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Section: Discussionmentioning

confidence: 99%

Elisa for Detecting Okadaic Aced in Model Systems Using Purified Polyclonal Antibodies

Dixon

Hamdy

Hayden

et al. 1997

Rapid Methods Automation Mic

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Purification and Properties of Extracellular Phytase from Bacillus sp. KHU-10

2001

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Bacillus species producing a thermostable phytase was isolated from soil, boiled rice, and mezu (Korean traditinal koji). The activity of phytase increased markedly at the late stationary phase. An extracellular phytase from Bacillus sp. KHU-10 was purified to homogeneity by acetone precipitation and DEAE-Sepharose and phenyl-Sepharose column chromatographies. Its molecular weight was estimated to be 46 kDa on gel filtration and 44 kDa on SDS-polyacrylamide gel elctrophoresis. Its optimum pH and temperature for phytase activity were pH 6.5-8.5 and 40 degrees C without 10 mM CaCl2 and pH 6.0-9.5 and 60 degrees C with 10 mM CaCl2. About 50% of its original activity remained after incubation at 80 degrees C or 10 min in the presence of 10 mM CaCl2. The enzyme activity was fairly stable from pH 6.5 to 10.0. The enzyme had an isoelectric point of 6.8. As for substrate specificity, it was very specific for sodium phytate and showed no activity on other phosphate esters. The Km value for sodium phytate was 50 microM. Its activity was inhibited by EDTA and metal ions such as Ba2+, Cd2+, Co2+, Cr3+, Cu2+, Hg2+, and Mn2+ ions.

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Interaction of Starfish Embryonic Cells with the Complex of Okadaic Acid and Monoclonal Antibody Specific to Okadaic Acid

Cited by 2 publications

References 3 publications

Elisa for Detecting Okadaic Aced in Model Systems Using Purified Polyclonal Antibodies

Elisa for Detecting Okadaic Aced in Model Systems Using Purified Polyclonal Antibodies

Purification and Properties of Extracellular Phytase from Bacillus sp. KHU-10

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