Dyy. Wan et al., INCREASED PLASMA PYRIDOXAL-5'-PHOSPHATE WHEN ALKALINE-PHOSPHATASE ACTIVITY IS REDUCED IN MODERATELY ZINC-DEFICIENT RATS, Biological trace element research, 39(2-3), 1993, pp. 203-210
It is generally believed that the zinc metalloenzyme alkaline phosphat
ase is required to hydrolyze phosphorylated forms of vitamin B-6 prior
to their use. To test this hypothesis, rats were fed a liquid diet co
ntaining either adequate or moderately low zinc during gestation and l
actation. Zinc deficiency was produced in darns evidenced by significa
nt reductions in zinc concentration of plasma (49%), liver (25%), and
femur (24%), and plasma alkaline phosphatase activity (48%). Plasma py
ridoxal-5'-phosphate (PLP), which significantly increased (61%) in the
se same rats, was negatively correlated (r = -0.74, P < 0.02) with pla
sma alkaline phosphatase activity. Maternal liver PLP concentration wa
s unaffected by zinc status. The zinc and vitamin B-6 relationship see
n in dams was less observable in offspring. Stimulation of erythrocyte
alanine aminotransferase activity by exogenously added PLP in vitro t
ended to be higher in both moderately zinc-deficient mothers and their
offspring, but the difference was not significant. Our results suppor
t the hypothesis that alkaline phosphatase activity is required for th
e hydrolysis of plasma PLP. Our results also suggest that zinc status
as alkaline phosphatase activity should be defined in an individual if
plasma PLP is to be used as an indicator of vitamin B-6 status.