Neutral calcium-activated proteases from European sea bass ( Dicentrarchus labrax L.) muscle: polymorphism and biochemical studies

• Published in: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 2000, Vol.125 (1), p.83-95
• Main Authors: Ladrat, Christine, Chaplet, Michael, Verrez-Bagnis, Véronique, Noël, Joëlle, Fleurence, Joël
• Format: Article
• Language: English
• Subjects: Animals; Bass - physiology; Biochemical properties; Calpain; Calpain - genetics; Calpain - metabolism; Dicentrarchus labrax; Enzyme Activation; Expression; Fish muscle; Gene Expression Regulation, Enzymologic - physiology; Hydrogen-Ion Concentration; Marine; Muscle, Skeletal - enzymology; Polymorphism; Polymorphism, Genetic; Post-mortem; Purification; Role; Seasonal variation; Seasons; Temperature
• ISSN: 1096-4959; 0305-0491; 1879-1107
• DOI: 10.1016/S0305-0491(99)00157-1

Calcium-dependent proteinases or calpains were studied in fish muscle. Hydrophobic chromatography, followed by anion-exchange chromatography of the soluble fraction of sea bass white muscle proteins, resulted in three peaks of calcium-dependent protease activity at neutral pH (A, B and C). They are all neutral cysteine calcium-activated proteinases and can, therefore, be classified as calpain-like enzymes. From the Ca 2+ concentration required for activity, A is a μ-calpain, and B and C are m-calpains. They share many properties with calpains from other vertebrate cells but differ in native mass, subunit composition, and the unusual numbers in which they are present. Their specific pattern of expression throughout the year could be of great importance to the resulting rate and extent of degradation of fish flesh after death.