The purpose of the present investigation was to study the acid-isomerization of monoterpene aldehydes and alcohols, such as dihydroperillaldehyde (I), phellandral (II), perillyl alcohol (III), dihydroperillyl alcohol (IV) and phellandrol (V), in connection with a previous report¹⁾ on the isomerization of perillaldehyde (VI).
Isomerization of each compound was conducted in 10% aqueous sulfuric acid in the same manner as previously described.¹⁾ Phellandral (II), however, was never isomerized within the limits of our experimental conditions.

View full abstract

A large amount of ammonia is produced in the rumen and some portion of the ammonia are absorbed into the portal blood through the rumen mucosa. Accordingly, it seems that ammonia detoxication is more necessary for the ruminant than for the nonruminant. Activities of the urea cycle enzymes as principal instrument for ammonia detoxication in goat were investigated in this experiment.
The activities of the urea cycle enzymes of goat were found to be very similar to those of rat reported by other authors. The activities of the urea cycle enzymes were affected by the protein level of diet. Administration of magnesium aspartate increased the activi-ties of argininosuccinate synthetase and arginase, and had some effect on the concentrations of citrulline, aspartic acid, and urea in the liver.

View full abstract

Changes in the time course of the urinary excretion of creatinine, creatine and urea, and the activities of kidney transamidinase and liver urea-cycle enzymes were investigated in rats fasted and fed on_??_10% casein diet and 10% casein diets supplemented with 10% glycine and/or 1.4% arginine.
The urinary total-creatinine of the fasted rats increased extremely during fasting for 7 days, while that of the animals given the 10% casein diet supplemented with glycine and arginine rose exceedingly on the 3rd day and thereafter no significant change was observed. Most of the increase of total-creatinine could be accounted for by the increase of creatine. The activity of kidney transamidinase in the fasted rats decreased in the 3rd day and thereafter kept nearly constant. The transamidinase activity of rats fed on the 10% casein diet after giving a protein-free diet for 5 days increased in the 3rd day. An inverse relation was observed between the urinary creatine and the transamidinase activity. The urinary urea increased in the rats fasted or fed on the 10% casein diets with the supplement of glycine and/or arginine. In fasting, the activities of liver urea-cycle enzymes, except arginase, had a tendency of increasing with the lapse of time. The arginase activity remained more or less constant. The reason of the extreme increase of urinary creatine during starvation was discussed.

View full abstract

An oligogalacturonate transeliminase (oligogalacturonate lyase) was isolated from the cell extract of Erwinia aroideal. This enzyme was purified by adsorption on columns of calcium phosphate on cellulose, treatment with Duolite CS-101 and DEAE-cellulose chromatography. It cleaved the first glycosidic linkage from the reducing end of the substrate molecule, the product found in the reaction mixture being 4-deoxy-5-keto-D-fructuronic acid. It attacked preferentially the short-chain uronides. The enzyme preparation showed only a slight activity toward high molecular pectic acid. The pH optimum was at 7.0. Calcium ion had no effect on the enzyme activity. Unsaturated oligogalacturonates were degraded more rapidly than oligogalacturonates having no unsaturated galacturonic acid residue. For this reason it might be appropriate to call this enzyme unsaturated oligogalacturonate transeliminase.

View full abstract

A strain of Streptomyces sp. produced little of uricase in the cells when they were grown in a medium consisted of peptone, glucose and inorganic salts, even in the presence of urate. The cells, however, formed a large amount of the enzyme, when they were incubated with urate in K-phosphate buffer. The amount of uricase thus formed was maximum by the cells which were harvested at the middle logarithmic phase of the preliminary growth. The induced formation of uricase required K ions in addition to Mg ions and was accelerated by glucose and some other carbon sources. The enzyme formation was inhibited completely by chloramphenicol at_??_low concentration. An equimolar allantoin to urate decomposed by the cells was accumulated in the incubation mixture. More than 3.0 units of uricase per g of wet cells were produced under the best conditions known from the present experiments. The derepression of uricase formation in the resting cells incubated in the phosphate buffer was discussed.

View full abstract

To search precursors of ethylene in banana fruits, ethylene formation from acetate-2-¹⁴C and fumarate-2, 3-¹⁴C by banana slices was studied. Ethylene-¹⁴C formation from acetate-2-¹⁴C was reduced by the addition of malonate or β-hydroxypropionate, and it was enhanced in a sealed chamber in comparison with the case in an aeration chamber. No label of fumarate-2, 3-¹⁴C was incorporated into ethylene.
From these facts it was suggested that acetate-2-¹⁴C was incorporated into ethylene via malonate and β-hydroxypropionate. Participation of fumarate in ethylene biosynthesis of banana fruits was ruled out. β-Hydroxypropionate was postulated as an effective precursor of ethylene formation from acetate-2-¹⁴C.

View full abstract

To elucidate the participation of β-hydroxypropionate in ethylene biosynthesis in banana fruits, ethylene formation in banana pulp slices and homogenates was examined by using propionate-2-¹⁴C as a tracer.
Optimum ethylene formation from propionate-2-¹⁴C was observed in the presence of Mg²⁺, TPP and NADP under an aerobic condition. It was also recognized that ethylene-14C formation from propionate-2-¹⁴C was diluted by β-hydroxypropionate. β-Hydroxy-propionate was proposed as a common precursor for ethylene formation from acetate-2-¹⁴C and from propionate-2-¹⁴C.
As a direct precursor of ethylene biosynthesis in banana fruits, acrylate was postulated.

View full abstract

An enzyme extract from ripe banana pulp catalyzed the formation of ethylene in the presence of Mg²⁺, TPP and acrylic acid under the gas phase of argon. Reactionconditions, cofactor requirement and optimum pH are presented.
Ethylene formation from acrylic acid catalyzed by TPP at pH 9.0 or by yeast decar-boxylase was also demonstrated.
The following route was proposed as a biosynthetic pathway of ethylene in banana fruit;
CO2
acetate→malonate→malonic semialdehyde→
β-hydroxypropionate→acrylic acid→ethylene+CO₂
NADP_??_NADP Mg²⁺, TPP
(NADPH₂, O₂)_??_(ffavin compoumd)
propionate

View full abstract

The lipid isolated from the fat globule membrane of milk was quickly autoxidized.The development of off-flavor like fishy flavor and brown color took place simultaneously. The browning material seemed to decompose fat peroxide. The addition of α-, γ and δ-tocopherol into the membrane lipid inhibited the formation of fat peroxide and off-flavor and decreased the browning degree. The addition of the membrane lipid prolonged the induction period of the oxidation of the milk fat obtained by churning. The antioxidant activity of α-, γ and δ-tocopherols added into the churned milk fat containing 1%of the membrane lipid was higher than that of the tocopherols added into the churned milk fat containing no membrane lipid.

View full abstract

Cells of Bacillus coagulans, strain HN-68 grown on the medium containing D-glucose, did not show any measurable D-glucose-isomerizing activity. However, when D-glucose-grown cells were shaked for a few hours in an induction medium containing D-xylose, induced formation of D-glucose-isomerizing enzyme occurred in the cells. Cell weight and number of survival cells showed only an increase of 30 and 10%, respectively during 6 hr induction.
The induced formation of D-glucose-isomerizing enzyme required organic nitrogen such as polypeptone in addition to D-xylose. Development of the maximum activity was observed when the concentration of D-xylose and polypeptone were 2 and 3 %, respectively. Initial velocity of induced formation of D-glucose-isomerizing enzyme increased in proportion to the decrease of initial pH values of the induction medium, i. e., at 2 hr induction, activity at pH 4.5 was 5-fold increase than that at pH 8.0.
Induced formation of D-glucose-isomerizing enzyme was inhibited strongly by addition of chloramphenieol, tetracycline, streptomycin, cyanide or azide, and was promoted by threonine plus glycine.

View full abstract

Biological availability of 106 esters of alcohols and aliphatic mono-, di- and tri-car-boxylic acids and diethylene glycol succinate was compared by the mini-test with chicks. Chicks can utilize methyl esters of saturated fatty acids of carbon chain from 10 to 14, ethyl esters of those from 9 to 12, propyl caprate, n-butyl esters of those from 8 to 12, n-amyl esters of those from 6 to 12, n-hexyl n-butyrate and i-valerate, and n-octyl and n-decyl acetates. Only 3 dicarboxylates, i. e. di-octyl and di-lauryl succinates and di-methyl cis-cyclopropane-l, 2-diearboxylate, were available among the dicarboxylates tested. Availability of ethyl esters of succinic, fumaric and citric acid was unexpectedly low.

View full abstract

Chicken feather keratin was solubilized by cupri-ethylenediamine treatment and the solubilized products were separated into acidic and basic fractions by ion exchangers. In the solubilized products which had a molecular weight between 10, 000 and 60, 000, all the original cystine residues disappeared and cysteic acid residues were recovered instead of them but partly. The cupri-ethylenediamine reagent which catalyzed air-oxidation of cystine residues in keratin was removable mostly from the products by dialysis against water. The common copper-amine complexes were ineffective to solubilize feather keratin except for Schweitzer's reagent. One strongly basic, unusual amino acid was detected in the basic solubilized fraction. This amino acid was eluted after arginine by usual column chromatography.

View full abstract

Succinoglucan, a succinylated polysaccharide produced by Alcaligenes faecalis var. myxogenes 1OC3, was partially hydrolyzed with acid. Fractionation of the neutral oligosaccharides gave cellobiose, gentiobiose, laminaribiose, laminaritriose, 6-O-β-laminaribiosylglucose, 6-O-β-laminaritriosylglucose, and 3-O-β-cellobiosylgalactose, confirming the previous results that the polysaccharide consists of β-(1→3)-linked, (1→4)-linked and (1→6)-linked D-glucose residues, and β-(1→3)-linked D-galactose residues.
Possible structural features of succinoglucan were discussed on the basis of the above and previous results obtained by Smith degradation.

View full abstract

When the usual assay method of proteinase using milk casein as substrate is applied to the crude extract of wheat bran culture of Aspergillus sojae KS, over 90% of the total activity at pH 7 to 8 is occupied by that of alkaline proteinase. However, lower hydrolytic activity of purified alkaline proteinase than that of crude extract was observed not only in the digestion of soybean meal but also in the digestion of soybean protein, in spite of the fact that each enzyme solution had the same proteolytic activity on milk casein. From the experiments to fractionate crude extract by chromatography on DEAE-Sephadex A-50, neutral proteinase I and II, whose contribution to the hydrolysis of milk casein was estimated to be under 10% of the total activity of crude extract, were suggested to have almost comparable effect to alkaline proteinase in the digestion, determined by the increase of 0.4M TCA-soluble nitrogen, of soybean protein by crude extract. Based on the rapid increase of 0.4M TCA-soluble nitrogen and slight increase of Formol-titration value, it seems that both neutral proteinase I and II act as endo-type enzyme similar to alkaline proteinase and are not effective in the liberation of low molecular peptides or amino acids.

View full abstract

Thirty five derivatives of sulfamoylphenyl phosphorothioate were prepared and their biological activities assayed by dipping method with Callosobruchus chinensis and by oral administration to mice to clarify the relationship between chemical structure and selective toxicity.
As a result, O, O-dimethyl O-[4-(N, N-diethylsulfamoyl)-3-chlorophenyl] phosphorothioate (Exp. No. S-4115) has the best properties as a low toxic insecticide in this series.
This compound (S-4115) was assayed with various insects as insecticide and with various plants for the phytotoxicity.

View full abstract

The volatile neutral compounds were collected from pork fat heated at 160_??_170°C for 3 hr under bubbling with air. They were analyzed by MS, GC and sometimes IR, and it was found that they consisted of 13 aldehydes, 2 ketones, 6 alcohols and 7 hydrocarbons. To elucidate one of the mechanisms of lactone formation in the flavor of heated meat fats, it was examined whether neutral compounds could be converted into lactones by heat. Lactones, which were identified through GC-MS analysis, was developed in trace amount from the heated undecane and not from 2t-decenal. It was expected through the quantitative estimation that the separated neutral compounds and undecane mixed with pork fats were converted into lactones.

View full abstract

The denaturation process of actomyosin during storage in 0.6M KCl at pH 5.7 and 25°C was studied by measuring ATPase activity, turbidity and solubility. During the storage of actomyosin the inactivation rate of myosin A ATPase was similar to that of the ATPase activating ability of F-actin. While the inactivation rate of isolated Factin was largely dependent on the initial protein concentration, that of F-actin in actomyosin was less dependent.
When F-actin was stored alone, inactivation of the ATPase activating ability was accompanied with a remarkable increase in turbidity and a decrease in solubility. However, this was not true when F-actin was stored with myosin A.

View full abstract

The denaturation process of actomyosin during storage in 0.6M KC1 at pH 5.7 and 25°C was studied with regard to changes in the binding ability of myosin A and actin.
When F-actin was stored alone, it lost the ability to bind with myosin A in pararell to the decrease in the ATPase activating ability. When myosin A was stored alone for 3hr, it maintained 60% of the initial ability to bind with F-actin, even if it lost 85% of the initial ATPase activity. Thus, the ATPase-less myosin A forms a myosin A-actin complex when it is mixed with intact F-actin. F-Actin was not stabilized in this modified myosin A-actin complex. This complex was dissociated with ATP into ATPase-less myosin A and intact F-actin.
The modified myosin A-actin complex did not occur in the stored actomyosin. During the storage of actomyosin, the interaction between myosin A and F-actin did not break and became less dissociable by ATP. This feature is in contrast with the one observed previously on the actomyosin stored in 0.6M KC1 at pH 5.7 and 3°C.

View full abstract