Expression of myofibrillar proteins and parvalbumin isoforms in white muscle of the developing turbot Scophthalmus maximus (Pisces, Pleuronectiformes)

• Main Authors: Focant, B., Collin, S., Vandewalle, P., Huriaux, F.
• Format: Article in Journal/Newspaper
• Language: English
• Published: 2000
• Subjects: Scophthalmus maximus; Turbot
• Online Access: https://www.vliz.be/imisdocs/publications/237950.pdf

Expression of polymorphic myofibrillar and sarcoplasmic proteins was investigated in the fish Scophthalmus maximus (L.) undergoing metamorphosis. A range of electrophoretic techniques was used to monitor sequential synthesis of isoforms from hatching to the adult stage. Two isoforms (larval and adult) of myosin light chain LC2 and troponin-I were successively detected during turbot growth, in addition to variations in the peptide composition of myosin heavy chains. Two isoforms of troponin-T also appeared sequentially, but the first to make its appearance was not detected until the juvenile stage. The composition of alkali light chains, actin, tropomyosin, and troponin-C did not seem to change as the fish progressed through the different stages. Parvalbumin isoforms were isolated and their physico-chemical parameters defined. As in the other fish examined so far, there appeared a succession of larval (PA IIa and PA IIb) and adult (PA V) parvalbumin isoforms through the life of the fish. All these biochemical changes occurred gradually in the course of turbot development, and did not appear particularly related to metamorphosis but rather to physiological needs of the different growth stages.