Electrophoretic comparison of myosin light chains and parvalbumins of trunk and head muscles from two barbel ( Barbus barbus) populations

• Published in: Comparative biochemistry and physiology. B, Comparative biochemistry Vol. 97; no. 3; pp. 547 - 553
• Main Authors: Huriaux, F., Vandewalle, P., Philippart, J.C., Focant, B.
• Format: Journal Article Web Resource
• Language: English
• Published: New York, NY Elsevier Inc 1990; Elsevier Science; Pergamon Press
• Subjects: Barbus barbus, wild fish, myosin; Biochemistry, biophysics & molecular biology; Biochimie, biophysique & biologie moléculaire; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; hatchery reared fish; Life sciences; parvalbumins, electrophoresis; Sciences du vivant; Striated muscle. Tendons; Vertebrates: osteoarticular system, musculoskeletal system; Trunk; Head; Growth; Barbus barbus; Red striated muscle; Contractile protein; Muscular fiber; Fecundation; Parvalbumin; Freshwater environment; Vertebrata; Electrophoretic mobility; Pisces; Myosin; Rearing; Circulatory system; White striated muscle
• ISSN: 0305-0491
• DOI: 10.1016/0305-0491(90)90158-P

1. 1. Myosin light chains and parvalbumins have been compared in several trunk and head muscles from small and large size barbels ( Barbus barbus) living in river or reared in hatchery. 2. 2. These proteins isolated from white, red and ventricle fibres exhibit identical electrophoretic characteristics in the four batches. 3. 3. The slow fibre content and the parvalbumin distribution are generally similar in river and hatchery barbels of the same size but differ between small and large barbels within a population. 4. 4. Alterations of the mode of fertilization and breeding conditions do not modify the differentiation of myosin and parvalbumins in barbels.