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Isolation and properties of sarcoplasmic reticulum from the fast muscles of plaice Pleuronectes platessa L.
Author(s) -
McArdle H. J.,
Johnston I. A.
Publication year - 1981
Publication title -
journal of fish biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.672
H-Index - 115
eISSN - 1095-8649
pISSN - 0022-1112
DOI - 10.1111/j.1095-8649.1981.tb02815.x
Subject(s) - endoplasmic reticulum , pleuronectes , calcium , biology , sarcoplasm , anatomy , medicine , biophysics , biochemistry , fishery , fish <actinopterygii>
This paper describes a method for the isolation of highly purified sarcoplasmic reticulum from plaice fast muscle. The interrelationships of pH, KCL, Ca 2+ , Mg 2+ , ADP and temperature have been investigated. Protein composition of plaice white muscle sarcoplasmic reticulum was found to be comparable to that described for rabbit fast muscle, with a major component of 100 000 daltons. Arrhenius plots of the Ca 2+ ‐AT Pase are linear over the range 0–30°C. Activation enthalpy (60±1.5 kJ/mol) was found to be independent of KCl concentration. The calcium concentration required to give half maximal activation of the AT Pase (K Ca ) was found to decrease with increasing temperature, from a maximum of 1.7 μm at 0°C to 0.55 at 20°C.