Scaling of atp-supplying enzymes, myofibrillar proteins and buffering capacity in fish muscle: Relationship to locomotory habit

Journal of Experimental Biology - Tập 149 Số 1 - Trang 319-333 - 1990
George N. Somero1,2, James J. Childress1,2
1Marine Biology Research Division, Scripps Institution of Oceanography, University of California, San Diego, La Jolla, CA 92093, USA and Marine Science Institute and Department of Biological Sciences, University of California, Santa Barbara, CA 93106, USA
2University of California 1 Marine Biology Research Division , , University of California, San Diego, La Jolla, CA 92093, USA and Marine Science Institute and Department of Biological Sciences , , Santa Barbara, CA 93106, USA

Tóm tắt

ABSTRACT Pelagic fishes with an ability to swim in strong bursts have previously been shown to have large size-dependent increases (positive allometric scaling exponents) in the activities of glycolytic enzymes in white skeletal muscle. This scaling of glycolytic activity has been hypothesized to provide the anaerobic power supporting the size-independence of relative burst swimming speeds (body lengths s−1) in these fishes. This paper presents tests of several predictions of this hypothesis, using different-sized individuals of two pelagic teleosts, the kelp bass (Paralabrax clathratus) and the freshwater rainbow trout (Salmo gairdneri), and a flatfish, the Dover sole (Microstomus pacificus). In the two pelagic species, an increase in body size was accompanied by an increase in activities in white muscle (i.u. g wet mass of muscle−1) of lactate dehydrogenase (LDH), an indicator of potential for anaerobic glycolysis, and creatine phosphokinase (CPK), an enzyme that helps maintain stable ATP concentration during muscular activity. Activities of citrate synthase (CS), an indicator of the potential for aerobic metabolism, decreased with size. In the flatfish, activities of all enzymes in white muscle decreased with body size, a trend proposed to reflect lack of adaptive value of strong burst swimming ability in this benthic fish. Activities of LDH and CS were size-independent in brain of flatfish, indicating that the scaling patterns observed in the muscle of this species were related to muscle function, not to common, organism-wide changes with size. In white muscle of P. clathratus, total protein and soluble protein concentrations and buffering capacity increased with body size in parallel, but myofibrillar protein was size-independent. These results suggest that the capacity for anaerobically powered work and the maximal potential to generate force scale only modestly in relation to total body mass and therefore do not appear to be functionally related to the pattern of glycolytic scaling. Thus, these data support the hypothesis that the functional role of the strongly positive scaling of glycolytic enzymes in the white muscle of pelagic fish is to provide increased power during burst swimming in larger-sized fishes.

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