Biomedical subjects
Publications and source records attributed to T Hama.
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We found X-prolyl dipeptidyl-aminopeptidase activity in rat brain and examined the developmental changes at various ages. The total enzyme activity per brain increased until 4 weeks of age, and then decreased during maturation. Specific activity in young rat brain was higher than that in adult rat brain. The properties of the brain enzyme were different from those of pituitary and other tissues.
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Anserine and carnosine in the muscle of growing rats were measured to explore the effect of dietary methionine. Carnosine was reduced in the gastrocnemius muscle of rats fed on a methionine-free diet. After refeeding on methionine for one week, carnosine in the muscle approached to the normal level. In contrast, anserine increased in the muscle of rats fed on a methionine-free diet. Anserine also increased in the gastrocnemius muscle of rats fed on a methionine-excess diet, whereas carnosine did not vary. Npi-Methylhistidine was detected in the muscle of rats fed on a methionine-excess diet. Moreover, Npi-methylhistindine and Ntau-methylhistine in the urine increased in the rats fed on both methionine-excess and methionine-free diets. Carnosine in the gastrocnemius muscle was not affected by a ethionine diet nor by a orotic acid diet which induced fatty liver. However, anserine increased in the muscle of rats fed on a ethionine diet.
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The molecular w:ight of yeast aldehyde dehydrogenase determined by sucrose density gradient centrifugation was 207,000 +/- 13,000. The enzyme activity was proportional to the enzyme concentration in the range of 2 X 10(-11) M to 1 X 10(-7) M. Cross-linking patterns obtained with yeast aldehyde dehydrogenase after treatment with a series of diimidoesters of increasing chain lengths with different reaction times resulted in the appearance of tetramers as the largest cross-linked product of the enzyme subunits. The molecular weights of its monomer, dimer, trimer, and tetramer were, 57,000, 114,000, 171,000, and 228,000, respectively, as estimated from their mobilities on SDS-electrophoresis. In tetramers monomers are probably assembled in a heterologous square arrangement.
X-Prolyl dipeptidyl-aminopeptidase activity was found in human urine by a sensitive fluorescence assay in which a new fluorogenic substrate, 7-glycylproline-4-methylcoumarinamide, is used. The Km value was 2.9 X 10(-4) mol/liter, and the optimum pH was 8.7 in glycine-NaOH buffer. The enzyme activity was stable at 4 degrees C for at least five days. On Sephadex G-200 column chromatography, normal human urine showed a main peak with an approximate relative molecular mass of 400 000. The procedure is simple, rapid, and accurate. The enzyme activity in urine of normal adults was: 4.30 +/- 0.13 (SE) (range, approximately 1.84-8.96) micronmol/min per gram of creatinine, and 2.16 +/- 0.09 (SE) (range, approximately 0.38-6.98) micronmol/min per liter of urine.
A procedure for the purification of aldehyde dehydrogenase from bakers' yeast (Saccharomyces cerevisiae) is reported. Treatment with acid, heat and organic solvents was avoided and chromatographic and filtration techniques in the presence of phenylmethylsulfonylfluoride were mainly used. An affinity chromatography step using the reactive dye Cibacron blue F3G-A, which was covalently bound to Sepharose 4B, was found to be essential. The enzyme was bound to and then released from the dye. The purified enzyme was shown to be homogeneous by gel filtration, disc electrophoresis and SDS electrophoresis. The molecular weight of the purified enzyme determined by gel filtration was 170,000, which agreed with that of the enzyme in the crude extract. The enzyme was composed of subunits of a molecular weight of 57,000. The specific activity of the enzyme was 20 units per mg of protein under the standard assay conditions. The substrate specificity, the relative maximal velocity, the michaelis constants, the pH optimum, the stability and the activation energy of the enzyme are reported.
Anserine and carnosine contents were determined in muscle of rats subjected to histidine depletion or excessive supplement. The contents of anserine and carnosine were reduced in the gastrocnemius muscle of rats fed a histidine-free diet. The diet showed especially a remarkable decrease of carnosine content. After rehabilitation for one week, the muscle anserine and carnosine contents in histidine-deficient rat returned to the normal level. The body and gastrocnemius muscle weight were decreased in rats fed a histidine-excess diet. However, anserine and carnosine content in muscle of rats fed a histidine-excess diet were twice of that of control rats. Urinary excretion of Npi-methylhistidine and Npi-methylhistidine was increased in rats fed a histidine-excess diet.
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Absorption beta-alanine, anserine or carnosine from rat intestine was studied in vivo by a force feeding method and in vitro using an everted sac method. Possibility of anserine and carnosine hydrolysis prior to intestinal absorption was also investigated using a glycylleucine dipeptidase-containing fraction prepared from rat intestine. The following results were obtained. 1) Anserine and carnosine were absorbed as they were from rat small intestine. 2) Both anserine and carnosine were partially hydrolyzed in vitro by the glycylleucine dipeptidase-containing fraction. Carnosine was hydrolyzed faster than anserine. The above rather conflicting results suggest that physiological amounts of anserine and carnosine might be absorbed from rat small intestine in dipeptide forms.
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