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 - http://www.scopus.com/inward/record.url?scp=0026703818&partnerID=8YFLogxK
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 Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
IS - 2
ER -