ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
SUMMARY: Skeletal muscle of brown trout contained one electrophoretically distinguishable lactate dehydrogenase (LDH) isozyme. In homogenates of the muscle, release of the enzyme into the soluble phase was favored by high ionic strength and high pH. DPNH solubilized the enzyme and prevented binding of soluble enzyme to particulate matter at concentrations which contributed only negligibly to the ionic strength of the suspending medium. The other compounds involved in the LDH-catalyzed reaction, DPN+, pyruvate, and lactate, were less effective. The effect of the latter two was due chiefly to their contribution to the ionic strength of the medium. Pyruvate, however, used with either DPNH or DPN+ exhibited a synergistic activity. Effective solubilization showed remarkable specificity for DPNH and TPNH. Solubilization by DPNH was also dependent on the tissue concentration of the suspending medium. The lower the tissue concentration, the more readily LDH is solubilized by DPNH. In addition to certain metabolic implications, this information may be used to define assay conditions to allow the study of the kinetics of LDH in bound and soluble forms.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1970.tb12370.x
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