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Molecular Pharmacology, Vol 15, 649-660, Copyright © 1979 by the American Society for Pharmacology and Experimental Therapeutics
1 Clinical Pharmacology Unit, Departments of Pharmacology and Internal Medicine,
Mayo Foundation, Rochester, Minnesota 55901
There are wide individual variations in the thermal stability of human plasma dopamine-
-hydroxylase (DBH) during incubation at 55°. When the ratio of enzyme activity after
heating at 55° for 20 minutes to that before heating (a heated-to-control, or H/C ratio)
was used as a measure of thermostabiity, 10.2% of frozen serum samples from 362
randomly selected subjects had relatively thermolabile DBH (H/C < 0.86). These subjects
also had a significantly lower average basal DBH activity (471 ± 49 units/ml, mean ±
SEM, N = 37) than that of the randomly selected subjects with more thermostable
enzyme (829 ± 25 units/ml, N = 325, p < 0.001). However, there was not a significant
correlation of the trait of thermolabile DBH (H/C < 0.86) with the presence of the
previously described allele for very low basal DBH enzymatic activity (< 50 units/ml).
The results of experiments in which plasma from subjects with thermolabile and thermostable DBH were mixed and experiments in which DBH was partially purified from
plasma by gel filtration chromatography were compatible with the conclusion that
variations in the structural properties of DBH itself were probably related to variations
in relative thermostability.