Two tissue-specific loci for octopine dehydrogenase in Tapes Decussatus (Bivalvia, Veneridae)

6533b7dafe1ef96bd126e989

RESEARCH PRODUCT

Two tissue-specific loci for octopine dehydrogenase in Tapes Decussatus (Bivalvia, Veneridae)

Andrea Santulli Andrea Santulli Noel P. Wilkins Vincenzo D'amelio

subject

Octopine biology Physiology D-octopine dehydrogenase Dehydrogenase Veneridae General Medicine Bivalvia biology.organism_classification Biochemistry Isozyme chemistry.chemical_compound Starch gel electrophoresis Biochemistry chemistry Botany Mantle (mollusc)Molecular Biology

description

Abstract 1. 1. Octopine dehydrogenase catalyses the reductive condensation of pyruvate and arginine to produce octopine in mollusc tissues. 2. 2. In all Bivalvia species studied to date, a single polymorphic locus, anodally migrating, was demonstrated. 3. 3. We studied, by starch gel electrophoresis, octopine isozymes in Tapes decussatus tissues. 4. 4. A polymorphic anodal form is present in adductor muscle, foot muscle, mantle and gill. 5. 5. A hepatopancreas-specific form, cathodally migrating, is also evident.

year	journal	country	edition	language
1992-06-01	Comparative Biochemistry and Physiology Part B: Comparative Biochemistry

https://doi.org/10.1016/0305-0491(92)90143-f

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