Isolation and properties of white skeletal muscle α-actinin from sea-trout (Salmo trutta) and bass (Dicentrarchus labrax)

Post mortem Release of Fish White Muscle α-Actinin as a Marker of Disorganisation

“…In a recent study (Papa et al 1995) we characterised bass and sea trout a-actinin and obtained very similar patterns in uitro proteolysis using the purified a-actinins and various proteinases. Moreover, we found in the present study, for both species stored at lWC, an a-actinin band of 88-89 kDa probably due to a Cterminal proteolytic action as described by Papa et al (1995). We also found smaller polypeptides that are not calpain products.…”

Dystrophin Cleavage and Sarcolemma Detachment are Early Post Mortem Changes on Bass (Dicentrarchus labrax) White Muscle

“…This part of titin was previously shown to bear an alpha-actinin binding site (Astier et al, 1992;Papa et al, 1995). The presence of calpain located in this myofilament anchor compartment (Goll et al, 1992) as the susceptibility of titin to in situ proteolysis induced by a thiol protease ( Kimura et al, 1993), seem to indicate the implication of a calpain isoform in this proteolysis.…”

Use of a Chaotropic Anion Iodide in the Purification of Z-Line Proteins: Isolation of CapZ from Fish White Muscle

“…Finally, this particular kind of chromatography is very effective when several proteins (namely actin, ␣-actinin, CapZ) are in tight interaction, as in the case of the arrangement of the Z-line proteins (9,21). Thus, we applied this procedure not only for CapZ purification, but also for that of ␣-actinin from the same tissue (5). In addition, it should be mentioned that ␣-actinin traces which usually contaminate actin preparation can easily be eliminated by this process (11).…”

“…The choice of KI was dictated by the fact that this anion generally preserves the native state of proteins (1,5,31). However, a limitation of the method can arise from the transformation of iodide into iodine, a wellknown oxidant.…”