The effect of high hydrostatic pressure and low temperature on lactic dehydrogenase and glutamic oxalacetic transaminase

LDH and GOT can be used with assurance as indicators of pressure-temperature effects in most regions of interest, specifically below 20,000 psi. LDH was susceptible to pressure deactivation at pressure levels below those tolerated by chymotrypsin, trypsin and alpha-amylase of Bacillus subtilis (17,...

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Veröffentlicht in:Cryobiology 1971-12, Vol.8 (6), p.524-534
Hauptverfasser: Carter, J.E., Graham, E.F., Lillehei, R.C., Blackshear, P.L.
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container_end_page 534
container_issue 6
container_start_page 524
container_title Cryobiology
container_volume 8
creator Carter, J.E.
Graham, E.F.
Lillehei, R.C.
Blackshear, P.L.
description LDH and GOT can be used with assurance as indicators of pressure-temperature effects in most regions of interest, specifically below 20,000 psi. LDH was susceptible to pressure deactivation at pressure levels below those tolerated by chymotrypsin, trypsin and alpha-amylase of Bacillus subtilis (17, 18, 20). Samples of LDH and GOT cooled to −20 °C were deactivated to the greatest extent by the application of pressure. The presence of glycerine and DMSO appeared to increase the sensitivity of GOT and LDH to pressure deactivation. When pressure was applied before cooling all pressures above 15,000 psi resulted in some deactivation of LDH and all pressures above 20,000 psi resulted in some deactivation of GOT.
doi_str_mv 10.1016/0011-2240(71)90003-4
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subjects Animals
Aspartate Aminotransferases
Cold Temperature
Dogs
In Vitro Techniques
Kidney - enzymology
L-Lactate Dehydrogenase
Perfusion
Pressure
Protein Denaturation
Solutions
Tissue Preservation
title The effect of high hydrostatic pressure and low temperature on lactic dehydrogenase and glutamic oxalacetic transaminase
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