A study has been made on growing rats to investigate the effect of variation in percentage of dietary protein calories from 0 to 50% by the use of purified whole egg protein on the growth, food efficiency, protein efficiency ratio (PER), body composition, and efficiencies of protein and energy utilization.
Body weight gain and PER attained a maximum, and food efficiency reached a plateau at 10PC% (protein calories percent) in the diet, having a constant metabolizable energy content (410kcal). Body and liver compositions changed in systematic patterns, where liver lipid content showed a specific increase at 5PC%.
Body protein retention reached a plateau at 15PC% but with little difference from the value at 10PC%, while body lipid retention give a maximum at 10PC% showing a gradual decrease thereafter.
Throughout the given dietary protein to energy ratios, energy utilization was constant when expressed as the increment of body energy retention divided by the increment of metabolizable energy intake. At and above 12 or 13PC%, the efficiency of net body protein energy retention against metabolizable energy intake was constant at about 12.5% on the average.

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1) The incorporation of ¹⁴C-methanol, ¹⁴C-formaldehyde, ¹⁴C-formate and ¹⁴C-bicarbonate into a methanol-utilizing yeast, Candida N-16, was examined by paper-chromatography and radioautography.
2) At the earliest time period examined, the highest percentage of radioactivity fixed from ¹⁴C-methanol or ¹⁴C-formaldehyde into methanol-grown cells was found in fructose phosphate. The percentage distribution of radioactivity in fructose phosphate decreased as time elapsed. The radioactivity fixed from these compounds into glucose-grown cells was negligible compared with that fixed into methanol-grown cells.
3) The incorporation of ¹⁴C-formate into methanol-grown cells was extremely low. The highest percentage of radioactivity fixed for short time incubation was found in serine. The incorporation pattern of glucose-grown cells was similar to that of methanol-grown cells.
4) At the earliest time period, over 70% of radioactivity fixed from ¹⁴C-bicarbonate into methanol- or glucose-grown cells was found in aspartate.
5) These results suggest that in Candida N-16 methanol is specifically assimilated by a route with hexose phosphate as a primary stable intermediate.

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The uptake and translocation of ¹⁴C-benthiocarb labelled at benzyl methylene by rice plant, barnyardgrass, wild amaranth, smart weed and lambsquarters were investigated. ¹⁴C-Benthiocarb was absorbed through the roots and the radioactivity was translocated into whole plants. The rate of absorption and translocation varied by the kind of plants. The translocation was occurred not only from roots into leaves, but from a leaf into other leaves, and even into roots of some kinds of plant. The absorption and translocation was more easy in barnyardgrass than in rice plant. Benthiocarb was rapidly absorbed by seeds and accumulated mostly in the embryo. The uptake of benthiocarb by seedlings decreased with the order of mesocotyl (barnyardgrass only), coleoptyl, root and leaf. Benthiocarb was degraded rapidly in plants.

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It has been shown that ovomucin, the structural glycoprotein of chicken egg white, has the inhibitory activity against aggregation of κ-casein by rennin.
The inhibitory activity of F-ovomucin, carbohydrate rich component, was much higher than that of S-ovomucin, carbohydrate poor component. The inhibitory activity was remarkably decreased by removal of sialic acid residues from ovomucin.

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From the reaction products of phosphatidyl ethanolamine and n-alkanals such as propionaldehyde or n-heptaldehyde at 60°C for 2hr, a series of phosphatidyl 1-(2-hydroxyethyl)2, 3, 5-trialkyl pyridiniums were isolated by silica gel column chromatography and were identified by the elementary analysis, UV, IR and NMR spectral analysis of alkali and acid hydrolyzates of the compounds. The course of formation reaction of pyridinium ring was discussed.

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3β-Hydroxysteroid oxidase (3β-hydroxysteroid: oxygen oxidoreductase, EC 1. 1. 3. 6.) from the culture supernatant of Brevibacterium sterolicum ATCC 21387 has a molecular weight of 32, 500 and an isoelectric point of 8.9. The enzyme contained 258 amino acid residues and the composition revealed a distinctive feature of a relatively high amount of proline and the absence of alanine and tryptophan. The crystalline enzyme exhibited an absorption spectrum characteristic of a flavoprotein with absorption maxima at 280, 390, and 470nm with a shoulder at 490nm. Anaerobic addition of dehydro-epi-androsterone as well as sodium dithionite to the enzyme produced a disappearance of the peaks at 390 and 470nm. The flavin moiety of the enzyme was isolated and identified as flavin adenine dinucleotide, I mole of which was found per mole of protein. The enzyme is sulfhydryl dependent and was inactivated by silver and mercury compounds. Analysis of the enzyme protein by atomic absorption spectrophotometry failed to detect any significant quantity of heavy metals.
Various 3β-hydroxysteroids were oxidized and the relative rates of the oxidation were cholesterol, 100; dehydro-epi-androsterone, 41; pregnenolone, 22; and β-sitosterol, 20. The oxidation product of cholesterol by the enzyme was crystallized and identified as 4-cholesten3-one by melting point, elementary analysis, optical rotation, UV, IR and NMR spectra. The oxidation of cholesterol proceeded as follows:
Cholesterol+O₂→4-cholesten-3-one+H₂O₂
The enzyme would be used for some analytical and preparative purposes in the field of steroid chemistry, e. g., microdetermination of cholesterol in serum.

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A highly purified trypsin inhibitor was obtained from the oriental plant Hakuhenzu bean (Dolichos lablab) by column chromatography on DEAE-Sephadex and gel-filtration on Sephadex G-75. The purified Hakuhenzu bean trypsin inhibitor (HTI) was obtained as a chemically homogeneous protein, and was stable to heat and to enzymes such as pepsin. It shows no obvious maximum at 280nm in the ultraviolet absorption spectrum, and it contains more than 20% carbohydrate as galactose and 10% hexosamine as glucosamine. The molecular weight of this inhibitor was determined to be approximately 9, 500 by gel-filtration. The protein contained 59 residures of amino acids; Lys₃, His₄, Arg₁, Asp₈, Thr₃, Ser₉ Glu₆, Pro₅, Gly₁, Ala₃, 1/2Cys₁₀, Val₁, Ile₁, Leu₂, Tyr₁, Phe₁, from which a molecular weight of 6, 400 is obtained. No methionine and tryptophan were found in the amino acid composition of the inhibitor. This inhibitor showed inhibitory activity against α-chymotrypsin in addition to trypsin.

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Forty-five new fluorinated acridines have been screened for their insecticidal activity against adult cockroaches (Periplanata americana), and six of them displayed significant activity.

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A variety of 6-substituted-3-pyridazinyl phosphorothioates were synthesized by the reaction of O, O-dialkyl phosphorothiochloridates with corresponding 3 (2H)pyridazinones. In certain cases, N-alkylated pyridazinones were formed along with the desired phosphorothioates. The optimal condition for the phosphorylation and the mechanism of the N-alkylation were investigated.

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Forty-three 3-pyridazinyl phosphorothioates were evaluated for insecticidal and acaricidal activities against two-spotted spider mite, turnip aphid, smaller brown planthopper, mosquito larvae and American cockroach. Approximate acute oral toxicity of these compounds in mice was also examined. In general, the toxicity in mice was in parallel with the pesticidal activity, but a few compounds clearly showed a high degree of selectivity between pests and mice. Especially O, O-dimethyl O-(6-cyclohexyloxy-3-pyridazinyl)phosphorothioate showed substantially reduced mammalian toxicity but maintained high insecticidal and acaricidal activity.

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A soy sauce sample was fractionated by gel filtration on a Sephadex G-15 column, then the fractions were subfractionated on the basis of acidity by ion exchange chromatography on a QAE-Sephadex A-25 column. After preliminary fractionation, the components in the neutral subfractions were transformed to copper salts, and the salts were chromatographed on a DEAE-Sephadex A-25 column with a borate buffer and aqueous acetic acid to separate neutral peptide substances from a large amount of free amino acids. The peptide fractions were further fractionated on a preparative amino acid analyzer and by paper chromatography to separate the peptide substances.
Three glycodipeptides and eight dipeptides were isolated and characterized as the major neutral peptide components in soy sauce. However, it was difficult to anticipate any direct contribution of these peptides to the flavor construction in soy sauce on the basis of their taste intensities and contents.

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A soy sauce sample was fractionated by gel filtration on a Sephadex G-15 column, then the fractions were subfractionated on the basis of acidity by ion exchange chromatography on a QAE-Sephadex A-25 column. The acidic subfractions with various acidities were further fractionated, using a preparative amino acid analyzer and by paper chromatography to separate the acidic peptide components.
Four dipeptides and sugar derivatives of ten dipeptides and two tripeptides were isolated and characterized as the major acidic peptides in soy sauce. However, it was difficult to anticipate any direct contribution of these peptides to the flavor construction in soy sauce on the basis of their contents and taste intensities.

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Production of erythritol by n-alkane-grown Candida zeylanoides KY 6166 was studied using large scale fermentors under conditions described in the previous report. The medium-pH was kept below 4.0 during fermentation in 5-liter or 300-liter fermentors. This strain produced about 180mg/ml of meso-erythritol and a small amount of mannitol. The yield corresponded to 90% of n-alkane consumed.
The production ratio between erythritol and mannitol was affected remarkably by the concentration of phosphate in the medium. Keeping its concentration at high level (0.04 to 0.20mg/ml as KH₂PO₄), erythritol production was almost entirely converted to mannitol production. The yield was 63mg/ml after 100 hr incubation in 5-liter fermentor, which corresponded to 52% of n-alkane consumed. Conversion of the production of erythritol to mannitol was also observed in several other yeasts capable of utilizing n-alkane as the sole source of carbon.

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A new spot test on silica gel thin-layers of some carbonyl compounds was described, which was based on their fluorigenic reactions with o-aminodiphenyl dissolved in diluted sulfuric acid. Pyridoxal, higher fatty aldehydes, glycolaldehyde, glyoxylic acid and 2, 3-pentanedione gave brilliantly fluorescent spots in UV light by heating with the reagent sprayed. Some other non- or sparingly volatile carbonyls also gave positive results.
The reaction of glyoxal with the reagent was carried out in aqueous solution. A linear relationship between the fluorescence intensity and glyoxal concentration was observed.

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The catalase activities of the Candida cells grown on hydrocarbons were generally much higher than those of the cells grown on lauryl alcohol, glucose or ethanol. Km values for hydrogen peroxide of the enzymes from the glucose- and the hydrocarbon-grown cells of Candida tropicalis were the same level. The enzyme activities of the yeasts were higher at the exponential growth phase, especially of the hydrocarbon-grown cells, than at the stationary phase. Profuse appearance of microbodies having homogeneous matrix surrounded by a single-layer membrane has also been observed electronmicroscopically in the hydrocarbongrown cells of several Candida yeasts. Cytochemical studies using 3, 3'-diaminobenzidine (DAB) revealed that the catalase activity was located in microbodies. These facts suggest that the catalase activities would be related to the hydrocarbon metabolism in the yeasts.

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1. The catalase activity of Candida tropicalis pK 233 was induced by hydrocarbons but not by glucose, galactose, ethanol, acetate or lauryl alcohol.
2. The induction of the catalase activity depending upon hydrocarbons was sensitive to cycloheximide but not to chloramphenicol.
3. Glucose repressed strongly the induction of the catalase activity by hydrocarbons but galactose did not affect seriously.
4. When C. tropicalis was incubated with hydrocarbons, the appearance of microbodies was observed electronmicroscopically.

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The main reaction product obtained when butylated hydroxyanisole (BHA) and trimethylamine oxide (TMAO) were thermally treated in liquid paraffin under a nitrogen stream at 180°C for 1 hr, was investigated. The crystalline substance obtained by the silica gel chromatography was recrystallized from ethanol and identified as the BHA dimer of biphenyltype, i.e., 2, 2'-dihydroxy-5, 5'-dimethoxy-3, 3'-di-tert-butyl biphenyl, by means of the elementary analysis and the spectroscopic studies.
The BHA dimer was found to be inferior to BHA in the antioxidative activity which was compared according to the weight gain method, in either case when lard (at 60°C) and methyl esters of linseed oil (at 30°C) were used as substrates. The dimer showed a synergism with TMAO.

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The discovery that anisomycin showed plant growth-regulating activity led to the investigation of compounds having p-methoxyphenyl group; the p-anisole derivatives. 4-Methoxydiphenylmethanes and related compounds inhibited the growth of both shoots and roots in test plants. Growth-inhibitory activity in the series of 4-methoxydiphenylmethanes was lowered by an increase in the electron. donating or withdrawing ability of the substituent and was parabolically dependent on the Hammett's σ. Selective actions of these compounds in their growth inhibition are discussed based on correlations between their activities against barnyard grass and other test plants.
Some 4-methoxydiphenylmethanes induced chlorosis, a disturbance in phototropism or geotropism, and root hypertrophy.

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The study was undertaken to clarify whether three kinds of lipases (EC 3. 1. 1. 3) secreted from Rhizopus delemar are originally different or identical with each other. First of all, the purification of those lipases was carried out and their enzymatic properties were examined. Their properties including the stability on heat and pH, precipitabilities at a certain pH, the behaviours on a SE-Sephadex C50 column and on a Sephadex G200 column and so on were compared.
From the results, A-lipase is clearly different from the other two lipases. On the other hand, it seems that B- and C-lipases are originally identical.

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Rhizopus (Rh.) delemar were cultivated under the various conditions and the productivity of three lipases (A, B, and C) were examined. There seemed to be no remarkable change of A-lipase production so far as examined, however, the productions of B- and C-lipases were changed with correlation depending on the composition of the medium. B-lipase was increasingly produced as much as C-lipase production decreased by the presence of phospholipid in a culture medium. The property of C-lipase was so changed by the incubation with phospholipid as to agree with that of B-lipase. Besides the above, the property of B-lipase was changed by its purification to that of C-lipase.
From these results, it seems that B-lipase protein is the same as that of C-lipase and a phospholipid is related to the intercoversion from C-lipase to B-lipase.

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