The regulation mechanism by calcium involved in the α-amylase formation of a certain Bacillus subtilis was investigated. The bacterial cells were found to associate with a large quantity of calcium, but in the association neither metal specificity nor energy de-pendence was observed. The calcium was quantitatively distributed in the cellular fraction sensitive to lysozyme and was found essential for the enzyme formation. The calcium present in protoplasts of the bacterial cells was not influenced by EDTA and did not seem to have an effect on α-amylase formation.

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Two species of sea-cucumber were found to contain an unknown saponin component besides the major one identical with holothurin A isolated by Chanley from Actinopyga agassizi. The unknown component was newly isolated and designated holothurin B. It holds D-quinovose, D-xylose, sulfuric acid as the sodium salt, and presumably the same aglycon in common with holothurin A but lacks 3-O-methyl-D-glucose and D-glucose present in the latter.

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Three new pigments, named versicolorins A, B and C, as metabolites from the mycelium of Aspergillus versicolor have been isolated. Versicolorin A, C₁₈H₁₀O₇, is fine orange yellow needles, m. p. 289°C (decomp.), [α]D-354°. It is an anthraquinoid pigment having three hydroxyl groups and a vinyl ether system contained in a five-membered ring. Versicolorin A trimethyl ether was hydrogenated to a dihydro-derivative, and by oxidation gave 3, 5-dimethoxyphthalic acid and a hydroxy acid which may be 1, 6, 8-trimethoxy-3-hydroxy anthraquinone-2-carboxylic acid. These chemical behavior and NMR data show that versicolorin A probably has the structure of (I). Versicolorin B, C₁₈H₁₂O₇, is fine orange yellow needles, m. p., 298°C (decomp.), [α]D-223° Its trimethyl ether is identical with that of dihydroversicolorin A. Therefore, the structure (II) could be assigned to versicolorin B. Versicolorin C, C₁₈H₁₂O₇, is orange red needles, m. p.>310°C, [α]D 0° Comparison of optical properties, IR and NMR spectra of versicolorin B and its methyl ether with those of versicolorin C and its methyl ether indicates that versicolorin C is very probably a racemate of versicolorin B.

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In order to clarify whether the myrosinase containes only thioglucosidase, or thioglu-cosidase and sulfatase, chromatographic behaviors of the myrosinase on cellulose ion exchanger were studied. Myrosinase showed two peaks by the chromatography on TEAE-cellulose at pH 8.5, but the fractionation of the two enzymes was not accomplished. It was concluded that the two peaks was not ascribable to an artifact but the two closely resembled species of myrosinase existing in the sample solution. Chromatographic separa-tion of the two enzymes on DEAE-cellulose resulted in failure. These results confirmed that the myrosinase was a single β-thioglucosidase originally.

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The mechanism of activation of plant myrosinase by ascorbic acid was studied. The oxidation-reduction reaction of ascorbic acid had nothing to do with the reaction by the activated myrosinase. Presence of firmely bound ascorbic acid in the enzyme protein was doubtful from the result of incubation with ascorbate oxidase. Presence of the effector site for ascorbic acid was presumed by the kinetic measurement and the instabilization by ascorbic acid in heating. But the effector site and the substrate site could not be distinguishable experimentally. The affinity of ascorbic acid to the myrosinase was not influenced by the substrate. The differences of the activation mechanism of the myrosinase by ascorbic acid and the allosteric enzyme were discussed.

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Pure (+)-trans-chrysanthemic acid was synthesized from (+)-Δ³-carene.
Ozonolysis of (+)-Δ³-carene affords 2, 2-dimethyl-3-(2-oxo-propyl)-cyclopropyl-acetalde-hyde which was cyclized to (-1-)-2-acetyl-6, 6-dimethyl-bicyclo-[3, 1, 0]-2-hexene. The bicyclo compound was transformed into (+)-cis-homocaronic acid by ozonolysis followed by oxid-ation. Diester or anhydride of the acid and methyl magnesium iodide gave (-)-dihydro-chrysanthemolactone which afforded finally (+)-trans-chrysanthemic acid via ethyl (-)-cis-chrysanthemate.

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Studies were made on the effect of water level of culture medium on the metabolism of organic acids and the distribution of pro-tease and α-amylase between the mycelia and culture medium.
1. Grown on the low water medium, the mold consumed much more organic acids especially citric acid in the medium. The composition of organic acids in the mycelia was also affected by the water level of the medium.
2. It was observed that much more protease and α-amylase were found in the medium than in the mycelia when the mold grew on the low water medium. It was shown that the mycelia grown on the low water medium were apt to release much more protease into the culture medium.

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The pH 4.5 soluble tryptic peptides of Holmes Rib-Grass strain virus protein were fractionated by Dowex 1×2 column chromatography and their amino acid compositions were determined. The purification of the peptides has been achieved by chromatography on Dowex-l×2 following paper chromatography. The sequences of five small peptides have been established. These are as follows. T-3; Asn-Arg, T-5; Asp-Thr-Val-Arg, T-6; Ser-Phe-Asp-Thr-Arg, T-7; Phe-Pro-Asp-Thr-Gly-Phe-Arg, T-9; Val-Asp-Asp-Ala-Thr-Val-Ala-Ileu-Arg.

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Whole casein, αs-casein and k-casein were dephosphorylated with a phosphoprotein phosphatase prepared from beef spleen and their calcium-binding capacities were compared with those of respective native caseins by a ultracentrifugal method.
The bindings of the calcium to 94% dephosphorylated whole casein and to 97% dephos-phorylated αs-casein at neutral pH were approximately one third of those to respective native caseins. The decrease of calcium-binding capacity of K-casein due to dephosphory-lation was also significant.
The effect of pH on the state and the calcium-binding capacity of dephosphorylated caseins was also examined and the role of organic phosphate groups of casein as calcium-binding sites was discussed.

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The action of the eighteen antibiotics on the growth of phage HM 2 of Clostridium saccharoperbutylacetonicum was studied by means of one-step growth technique as a part of basic study for preventing phage-infection in industrial fermentation. Three antibiotics (even 100μg/ml) had no effect upon the growth of phages and bacteria. Fourteen antibiotics were effective against both, and the effect of these antibiotics on the phage growth closely paralleled that on bacterial growth.
Of the antibiotics tested, only chloramphenicol (CP) showed selective inhibition of phage growth, i.e., CP (ca. 1μ/ml) inhibited completely the phage growth, whereas it (up to 100μg/ml) failed to inhibit the growth of uninfected host bacteria. No phage yield occurred even when CP was added late in the latent period (within 40min.). Addition of CP after that time resulted in inhibition of further phage growth. CP had no direct phagicidal action, did not prevent adsorption and injection and did not inhibit lysis of infected cells. When CP was added in any time of latent period, protein synthesis in infected cells was stopped immediately, whereas total DNA continued to rise but at a reduced rate. These results indicate that CP inhibits the intracellular phage growth by suppressing the protein synthesis in infected cells.
CP inhibited also the growth of elevent HM-phages other than HM 2.

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Growth of an adenine-requiring yeast and a baker's yeast was markedly inhibited by the addition of methionine to culture media. The inhibition was reversed by adenine or more clearly by adenine plus glucose supplements. The inhibition by methionine of the adenine-requiring yeast was more pronounced when the media contained relatively low levels of adenine. Further addition of adenine to the media reversed the inhibition. It appears, therefore, that methionine is a competitive inhibitor of adenine for growth of the yeast cells.

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The nutritional values of 16 D-amino acids in chick growth were studied on the purified diets containing crystalline amino acids as a sole source of nitrogen. Growth rate, feed consumption and nitrogen retention were measured. The nutritional values of D-amino acids were studied by comparing individually with the control groups fed on the diet containing all L-amino acids and negative control groups fed with the diet omitted the cor-responding L-isomer. The following results were obtained. Essential amino acids: 1. Equal or almost equal nutritional value to the corresponding L-isomer; methionine, phenyl-alanine, leucine, proline. 2. Half nutritional value compared with L-isomer; valine. 3. Small nutritional value compared with L-isomer; tryptophan, isoleucine, histidine. 4. No nutritional value; lysine, threonine, arginine. Non-essential amino acid: 1. Equal or almost equal nutritional value to the corresponding L-isomer; serine, tyrosine, cystine. 2. There is a possibility that it has a slight growth retardation effect; alanine. 3. The growth retardation effect was found; aspartic acid.

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A glycoside “Sasanquin” was separated from methanol extract of young leaves of Camellia sasanqua Thunb. It was not able to be found in young leaves of Camellia japonica L. and Thea sinensis L. on paper chromatogram. Investigations showed that this glycoside is composed of eugenol, D-glucose and D-xylose, and it has a structure of 3-methoxy-4-β-primeverosidoxy-allylbenzene.

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The properties of crude phosphodiesterase forming 5'-mononucleotide of Pellicularia H-11 were investigated on its metal requirement, pH response for activity and so on. The dialyzate of crude PDase against distilled water became partly inactive, but was recovered with Zn⁺⁺, Mn⁺⁺ and Mg⁺⁺, whereas completely inactivated dialyzate against EDTA was restored specifically with only Zn⁺⁺
The optimum pH of PDase activity was 5.0 and that of ribonuclease 4.0. The crude PDase was partially purified by acetone fractionation and Amberlite IRC-50 (XE-64) or CM-cellulose column chromatography. Two PDase and a RNase activities were recognized.
Pellicularia PDase was found to be of new type according to its Zn⁺⁺ dependency and non-activity towards bis-p-nitrophenyl phosphate.

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In the presence of oxygen, L-ascorbic acid solution (0.05_M) browned more intensely than dehydro-L-ascorbic acid solution (0.05_M) during storage for longer period.
The mixed solution of L-ascorbic acid (ASA) and dehydro-L-ascorbic acid (DHA) with the ratio of 1:1 or 1:3 in concentration gave more intense browning than DHA solution during storage at 38°C for about 3 weeks. Essentially the same type of browning was observed in case of the mixture of ASA and DHA with D-glucose. Browning of partially oxidized ASA solution also showed substantially the same results as those mentioned above.

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A New method was devised for the estimation of the mycelial weight in rice-koji. In this method, the content of glucosamine in koji was used for the calculation of mycelial weight. The content of glucosamine in the mycelia of Aspergillus oryzae, koji, and rice was determined by a colorimetry after hydrolysis of these materials with sulfuric acid and purification of glucosamine fraction with a Dowex 50W column. And the values of glucosamine were 114.5mg/g in mycelia, 3.03 in the koji for amazake, ^* 1.34 in the koji for sake, and 0.0 in rice. The mycelial contents calculated from these data were 2.60 dry weight in amazake-koji and 1.2% in sake-koji.

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γ-Glutamyltranspeptidase activity during germination of soybean was very low in 0_??_24 hours of germination, but reached a maximum in 40_??_48 hours and decreased remarkably after 72 hours. The change in activity agreed with the variations in the amount of γ-glutamyltyrosine and γ-glutamylphenylalanine during germination.

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