Eight commercially available organic Zn products and reagent-grade ZnSO4 x 7H2O (Zn Sulf) were evaluated by polarographic analysis, and solubility in .1 M K2HPO4-KH2PO4 buffer (pH 5), .2 M HCl-KCl buffer (pH 2), and deionized water. Fractions from these solubility tests were evaluated by gel filtration chromatography for structural integrity. Degree of chelation was generally positively related to chelation effectiveness determined by polarography. The organic sources were Zn methionine complex A (Zn MetA), Zn methionine complex B (Zn MetB), Zn polysaccharide complex (Zn Poly), Zn lysine complex (Zn Lys), Zn amino acid chelate (Zn AA), Zn proteinate A (Zn ProA), Zn proteinate B (Zn ProB), and Zn proteinate C (Zn ProC). Three experiments were conducted to estimate the relative bioavailability of Zn from the organic Zn supplements for chicks and lambs when added at high dietary levels to practical diets. Bone Zn concentration increased (P < .001) as dietary Zn increased in both experiments. When Zn Sulf was assigned a value of 100% as the standard, multiple linear regression slope ratios of bone Zn from chicks fed 3 wk regressed on dietary Zn intake gave estimated relative bioavailability values of 83 +/- 14.6 and 139 +/- 16.9 for Zn AA and Zn ProA, respectively, in Exp. 1 and 94 +/- 11.6, 99 +/- 8.8, and 108 +/- 11.4 for Zn Poly, Zn ProB, and Zn ProC, respectively, in Exp. 2. In Exp. 3, 42 lambs were fed diets containing Zn Sulf, Zn ProA, Zn AA, or Zn MetB for 21 d. Based on multiple linear regression slope ratios of liver, kidney, and pancreas Zn and liver metallothionein concentrations on added dietary Zn, bioavailability estimates relative to 100% for Zn Sulf were 130, 110, and 113 for Zn ProA, Zn AA, and Zn MetB, respectively. Except for Zn ProA, which was greater, the organic Zn supplements had bioavailability values similar to that of Zn Sulf for chicks and lambs. Bioavailability of organic Zn products was inversely related to solubility of Zn in pH 5 buffer in chicks (r2 = .91) and pH 2 buffer in lambs (r2 = .91), but not to an estimate of degree of chelation.

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The appearance of both [(2)H(1)]- and [(2)H(2)]methionine forms indicates that both cytosolic and mitochondrial metabolism of exogenous serine generates carbon units in vivo for methyl group production and homocysteine remethylation. This study also showed the utility of serine infusion and indicated functional roles of cytosolic and mitochondrial compartments in one-carbon metabolism.

Vitamin B-6 deficiency causes mild elevation in plasma homocysteine, but the mechanism has not been clearly established. Serine is a substrate in one-carbon metabolism and in the transsulfuration pathway of homocysteine catabolism, and pyridoxal phosphate (PLP) plays a key role as coenzyme for serine hydroxymethyltransferase (SHMT) and enzymes of transsulfuration. In this study we used [(2)H(3)]serine as a primary tracer to examine the remethylation pathway in adequately nourished and vitamin B-6-deficient rats [7 and 0.1 mg pyridoxine (PN)/kg diet]. [(2)H(3)]Leucine and [1-(13)C]methionine were also used to examine turnover of protein and methionine pools, respectively. All tracers were injected intraperitoneally as a bolus dose, and then rats were killed (n = 4/time point) after 30, 60 and 120 min. Rats fed the low-PN diet had significantly lower growth and plasma and liver PLP concentrations, reduced liver SHMT activity, greater plasma and liver total homocysteine concentration, and reduced liver S-adenosylmethionine concentration. Hepatic and whole body protein turnover were reduced in vitamin B-6-deficient rats as evidenced by greater isotopic enrichment of [(2)H(3)]leucine. Hepatic [(2)H(2)]methionine production from [(2)H(3)]serine via cytosolic SHMT and the remethylation pathway was reduced by 80.6% in vitamin B-6 deficiency. The deficiency did not significantly reduce hepatic cystathionine-beta-synthase activity, and in vivo hepatic transsulfuration flux shown by production of [(2)H(3)]cysteine from the [(2)H(3)]serine increased over twofold. In contrast, plasma appearance of [(2)H(3)]cysteine was decreased by 89% in vitamin B-6 deficiency. The rate of hepatic homocysteine production shown by the ratio of [1-(13)C]homocysteine/[1-(13)C]methionine areas under enrichment vs. time curves was not affected by vitamin B-6 deficiency. Overall, these results indicate that vitamin B-6 deficiency substantially affects one-carbon metabolism by impairing both methyl group production for homocysteine remethylation and flux through whole-body transsulfuration.