caa a22 4500 465826423 CHVBK 20180323112150.0 cr unu---uuuuu 170327e19900401xx s 000 0 eng 10.1007/BF00258759 doi (NATIONALLICENCE)springer-10.1007/BF00258759 Temperature acclimation and the expression of contractile protein isoforms in the skeletal muscles of the common carp ( Cyprinus carpio L.) [Elektronische Daten] [Tony Crockford, Ian Johnston] Summary: Common carp (Cyprinus carpio L.) were acclimated to either 2, 5, 8, 11, 15, 20, or 23°C for 12 weeks (12 h light: 12 h dark). Fish did not feed after 6 weeks at temperatures below 8°C. Skinned fibres were prepared from fast myotomal muscle by freeze-drying. Measured at 0°C unloaded contraction velocity (Vmax) and maximum isometric tension generation (Po) were 2-3 times higher in the 11°C-than 23°C-acclimated groups, and had intermediate values in 15 °C-acclimated fish. Po and Vmax at 0°C were not significantly different for carp maintained at 2, 5, 8, or 11°C. Measured at the acclimation temperature of each group Vmax and Po were 51% and 71% lower for fibres from 2°C- than 23°C-acclimated fish. The results indicate a partial capacity adaptation of muscle power output in fish acclimated between 11°C and 23°C. At 8°C the ATPase activity of myofibrils was 2 times higher in fish acclimated to 8°C than to 20°C. The effects of temperature acclimation on the protein composition of myofibrils was investigated using one- and two-dimensional electrophoresis. Peptide maps of purified myosin heavy chains and actin prepared by proteolytic digestion with either Staphylococcus aureus V8 protease or chymotrypsin were similar for both acclimation groups. The molecular weights and isoelectric points of the major isoforms of tropomyosin, troponin C, troponin I, troponin T, and myosin light chains (MLC1, MLC2 and MLC3) were also similar in 8°C- and 20°C-acclimated carp. A 20 kDa molecular weight protein with a pI intermediate between that for MLC2 and MLC3 was found in myofibrils and single fibres from carp acclimated to 8°C but was not present in carp acclimated to 20°C. It is suggested that this band corresponds to a myosin light chain isoform unique to cold-acclimated fish. Evidence was also obtained that myofibrils from warm-acclimated fish contained a second minor isoform of troponin I. Springer-Verlag, 1990 Fish-skeletal muscle nationallicence Temperature acclimation nationallicence Contractile properties nationallicence Myofibrillar proteins nationallicence Crockford Tony Gatty Marine Laboratory, Department of Biology & Preclinical Medicine, University of St. Andrews, KY16 8LB, St. Andrews, Fife, Scotland, U.K. aut Johnston Ian Gatty Marine Laboratory, Department of Biology & Preclinical Medicine, University of St. Andrews, KY16 8LB, St. Andrews, Fife, Scotland, U.K. aut Journal of Comparative Physiology B Springer-Verlag 160/1(1990-04-01), 23-30 0174-1578 160:1<23 1990 160 360 https://doi.org/10.1007/BF00258759 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00258759 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Crockford Tony Gatty Marine Laboratory, Department of Biology & Preclinical Medicine, University of St. Andrews, KY16 8LB, St. Andrews, Fife, Scotland, U.K aut NATIONALLICENCE 700 1- Johnston Ian Gatty Marine Laboratory, Department of Biology & Preclinical Medicine, University of St. Andrews, KY16 8LB, St. Andrews, Fife, Scotland, U.K aut NATIONALLICENCE 773 0- Journal of Comparative Physiology B Springer-Verlag 160/1(1990-04-01), 23-30 0174-1578 160:1<23 1990 160 360 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer