• Journal of Nutrition and Health
• /
• 제29권3호
• /
• pp.260-266
• /
• 1996

Eighteen crossbred pigs were weaned at 4 days of age and fed up to 28 days of age to examine the effect of sulfur amino acid content of three diets upon plasma taurine concentration and hepatic cysteinesulfinate decarboxylase activity. The experimental diets consisted of either whey protein (W) or partialy hydrolyzed soy protein (S) as the source of protein. 0.25% methionine was added to the S diet for the third dietary regimen (SM). Sulfur amino acid content(methionine plus cystine)of the three diets was 1.53%, 1.34% and 1.09% for the W, SM and S diet, respectively. Plasma taurine concentration from the pigs fed the three experimental diets reflected the total sulfur amino acid content of the diet. The S diet resulted in a significantly lower plasma tarrine level than the W and SM diets throughout the experiment. After three weeks, pigs fed the W diet had significantly higher plasma taurine concentration than those fed SM diet. Therfore it appears that taurine requirement of the pig depends on the sulfur amino acid contents of the diets and the conversion o sulfur amino acid to taurine seemed not to be limited by any factor when sulfur amino acid was below 1.53% of the diet. There was no significant difference between three dietary groups in hepatic cysteinesulfinate decarboxylase activity and this suggests that the reduced cysteinesulfinate decarboxylase activity due to high sulfur amino acid in the diet may not occur in the pig liver.

• BMB Reports
• /
• 제29권4호
• /
• pp.335-342
• /
• 1996

Porcine liver cysteinesulfinic acid decarboxylase was purified approximately 460-fold by means of ammonium sulfate fractionation and sequential column chromatographic separation with Sephadex G-100, DEAE-cellulose and hydroxylapatite. The enzyme has a flat pH profile with maximum activity occurring between pH 6.0 and 7.6. Pyridoxal 5'-phosphate must be present in all buffers used for purification procedures in order to stabilize the enzyme. Addition of sulfhydryl reagents such as 2-mercaptoethanol are also necessary to maintain maximum enzyme activity throughout purification. The absorption spectrum shows that cysteinesulfinic acid decarboxylase is a pyridoxal 5' -phosphate-containing protein. The major absorption is at 280 nm with two smaller absorption regions, one at 425 nm which is ascribed to a Schiffs base between pyridoxal phosphate and protein, and another at 325 nm which is thought to be due to the interaction of 2-mercaptoethanol with the Schiffs base. A number of divalent cations tested did not affect enzyme activity with the exception of mercury, copper, and zinc which are inhibitory. The partially purified enzyme has an apparent $K_m$ of 0.94 mM for cysteinesulfinate. Cysteic acid is a competitive inhibitor of the enzyme with a $K_i$ of 1.32 mM. The molecular weight of the enzyme was estimated to be about 79,600 by using Sephadex G-200 column chromatography.