Table 1.
Content and catalytic efficiency of LDH in muscle homogenates of fish species with different degree of piezophilic adaptation. a
| Species | LDH content, pmol·mg−1 protein b | Protein content in homogenate, mg·mL−1 | LDH concentration in homogenate, nm | Activity of LDH in homogenate, µm·s−1 c | LDH turnover at 1 bar pressure, s‐1 |
|---|---|---|---|---|---|
| L. florae | 16.8 ± 1.8 | 0.75 ± 0.28 | 12.5 ± 2.4 | 47.6 ± 19.4 | 4120 ± 620 |
| C. armatus | 129 ± 28 | 0.72 ± 0.16 | 92.5 ± 15.9 | 87.7 ± 35.6 (0.07) | 987 ± 168 |
| N. kermadecensis | 39.7 ± 8.1 | 0.63 ± 0.25 | 25.0 ± 5.6 | 50.0 ± 26.9 (0.89) | 2240 ± 450 |
| P. swirei | 68.7 ± 8.6 | 0.76 ± 0.18 | 52.0 ± 7.1 | 65.3 ± 25.2 (0.30) | 1640 ± 252 |
The values given in the Table were obtained by averaging results of 3‐6 individual measurements with different samples of fish muscle homogenates and the ‘±’ values show the confidence interval calculated for P = 0.05.
Content of LDH in muscle homogenate determined with mass‐spectroscopic determination of LDH‐specific peptide LNLVQR in tryptic lysates.
Calculated from LDH activity measured at atmospheric pressure (1 bar) at 5 °C and correspond to the µmols of NADH consumed per second per liter of undiluted homogenate. The values in parentheses represent the P‐values of Student’s t‐test for the hypothesis of equality of the respective values of LDH activity to that observed in muscle homogenates from L. florae.