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

Andrea Santulli; Noel P. Wilkins; Vincenzo D'Amelio

doi:10.1016/0305-0491(92)90143-F

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

Andrea Santulli
, Noel P. Wilkins
, Vincenzo D'Amelio

Zoology

University of Palermo
Libera Universitá del Mediterraneo

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

1 Citation (Scopus)

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.

Original language	English
Pages (from-to)	409-411
Number of pages	3
Journal	Comparative biochemistry and physiology. B, Comparative biochemistry
Volume	102
Issue number	2
DOIs	https://doi.org/10.1016/0305-0491(92)90143-F
Publication status	Published - Jun 1992

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

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.",

author = "Andrea Santulli and Wilkins, \{Noel P.\} and Vincenzo D'Amelio",

year = "1992",

month = jun,

doi = "10.1016/0305-0491(92)90143-F",

language = "English",

volume = "102",

pages = "409--411",

journal = "Comparative biochemistry and physiology. B, Comparative biochemistry",

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number = "2",

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TY - JOUR

T1 - Two tissue-specific loci for octopine dehydrogenase in Tapes Decussatus (Bivalvia, Veneridae)

AU - Santulli, Andrea

AU - Wilkins, Noel P.

AU - D'Amelio, Vincenzo

PY - 1992/6

Y1 - 1992/6

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/0026703818

U2 - 10.1016/0305-0491(92)90143-F

DO - 10.1016/0305-0491(92)90143-F

M3 - Article

AN - SCOPUS:0026703818

SN - 0305-0491

VL - 102

SP - 409

EP - 411

JO - Comparative biochemistry and physiology. B, Comparative biochemistry

JF - Comparative biochemistry and physiology. B, Comparative biochemistry

IS - 2

ER -

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

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