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Caryospora cheloniae sp. n. is described from mariculture-reared green sea turtles (Chelonia m. mydas). The sporulated oocyst has a thin, transparent, single-layered wall which often ruptures, leaving a naked sporulated sporocyst. Oocysts measured 33.8 to 40.1 micrometer by 11.0 to 14.6 micrometer (mean 37.4 by 12.8 micrometer). Greatest concentrations of(More)
A kinetically homogeneous anti-phosphate catalytic antibody preparation was shown to catalyse the hydrolysis of a series of O-aryl N-methyl carbamates containing various substituents in the 4-position of the O-phenyl group. The specific nature of the antibody catalysis was demonstrated by the adherence of these reactions to the Michaelis-Menten equation,(More)
The substrate selectivities of an anti-phosphonate and an anti-phosphate kinetically homogeneous polyclonal catalytic antibody preparation and two hydrolytic enzymes were compared by using hapten-analogous and truncated carbonate and ester substrates each containing a 4-nitrophenolate leaving group. Syntheses of the truncated substrates devoid of(More)
We report the first example of a monoclonal antibody-catalysed hydrolysis of a beta-lactam where the antibodies were generated by a simple transition-state analogue. A rat monoclonal antibody (1/91c/4d/26) generated by using an acyclic 4-nitrophenylphosphate immunogen catalysed the hydrolysis of corresponding 4-nitrophenyl carbonates but, more importantly,(More)
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