Isolation of microorganisms capable of synthesising amino acids, utilizing hydrocarbons, has been reported. These microorganisms were isolated from soil samples by selective culture techniques. 91 strains were found capable of producing amino acids in the broth. Different amino acids and their maximum yield obtained were glutamic acid 160mg/l; leucine 90.0mg/l; isoleucine 40.0mg/1; valine 105.0mg/l; methionine 25.0mg/l; tryptophan 2.5 mg/l; arginine 70.0mg/l; and histidine 10.0mg/l.

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Ovicidal and chemical properties of many analogs of 2-bromoethylthiobenzenes were investigated. Replacement of the sulfur atom of 2-bromoethylthiobenzenes by an oxygen atom or a sulfone group, and that of the ethylene group by a trimethylene or a tetrame-thylene group lowered both the ovicidal activity and the chemical reactivities. Branching of methyl group(s) in the ethylene chain of a certain substituted 2-bromoethylthiobenzenes extremely enhanced the chemical reactivities, but lowered the ovicidal activity of the parent compound.

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The volatile compounds such as acetaldehyde, propionaldehyde, acrolein, acetone, di-acetyl, furan, furfural and 5-methyl furfural from cellulose, cellobiose, glucose and levo-glucosan pyrolysates at 250°C, 350°C and 500°C were studied by gas chromatography with a pyrolyzer without intermediate trapping. The composition of the volatiles was changed with the temperatures and the degradation stages of cellulose pyrolysis.
Analytical data of the relative amounts of the volatiles show that pyrolysis of cellulose proceeds through two primary simultaneous reactions: a) the initial scission of glucosidic linkages, and b) chemical changes in anhydroglucose units of cellulose.

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The accumulation of S-adenosylmethionine in adenine-requiring yeast cells grown in a culture medium containing DL-, L-, or D-methionine was much larger than that in cells grown in a methionine-free medium. The accumulation of S-adenosyl-D-methionine in the cells was significantly lower than that of S-adenosyl-L-methionine. When yeast cells containing a large amount of S-adenosyl-L-methionine were incubated in an adenine-free medium, adenosylmethionine was degraded, but poor and insignificant growth was observed indicat-ing the meager nature of this compound as an adenine source. No degradation of accumulated S-adenosyl-D-methionine was detected. Isotopic experiment revealed that S-adenosyl-L-methionine in the yeast cells turned over at a considerable rate when the medium contained both adenine and L-methionine. Most of the L-methionine assimilated appears to be metabolized via S-adenosyl-L-methionine.

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The arginase activity of the liver of rats was measured after they had been maintained for 11 or 12 days on diets containing natural proteins (casein or gluten) or amino acid mixtures of various tryptophan levels.
Specific activity or total arginase activity increased with the increasing protein quality. Liver arginase activity of the casein group was significantly higher than that of the gluten group in every case for 27-, 61-, and 158-day-old rats. In the case of amino acid diets, the arginase increased with the increments of tryptophan levels up to the “tentative” minimum requirement in the diet. Moreover, these alterations in arginase activity varied inversely with the urinary urea excretion.
From the results, it was assumed that the total activity of liver arginase is not neces-sarily determined only by the metabolic needs for urea biosynthesis.

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The condensation of 4-formyltropolone (II) and 3, 4, 5-trimethoxybenzoyl-acetate (III) afforded β-[1-hydroxy-3-oxo-3-(3', 4', 5'-trimethoxyphenyl)-propy]-tropolone (IV) which was dehydrated to β-[3-oxo-3-(3', 4', 5'-trimethoxyphenyl)-1-propenyl]-tropolone (V). Catalytic hydrogenation of V gave β-[3-oxo-3-(3', 4', 5'-trimethoxyphenyl)-propyl]-tropolone (VI), which was further reduced to β-[3-hydroxy-3-(3', 4', 5'-trimethoxyphenyl)-propyl]-tropolone (VII). The distillation of VII afforded finally β-[3-(3', 4', 5'-trimethoxyphenyl)-2-propenyl]-tropolone (VIIIa). As the route to colchicine (I) from the tropolone (VIIIa) has already been exploited, ¹⁾ this shows a total synthesis of colchicine from 4-formyltropolone.

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The inactivation of Bacillus subtilis' α-amylase by acid was shown to be reversible. In the experiment, two different Bac. subtilis' α-amylases, saccharifying and liquefying types, were used and the reversibility was investigated deviding into two processes of inactivation and reactivation. Both amylases showed the reversibility in a similar degree and in general the inactivated enzymes by acid were reactivated only by adjusting the pH to slightly alkaline values followed by incubation under certain conditions. However, the reversibility, especially, the reactivation was greatly influenced by several chemicals, the effect of certain chemicals being different according to the type of the bacterial amylase. Contrary to liquefying amylase, saccharifying amylase was insensitive to metal chelators but, nevertheless, the reactivation of the amylase was prevented by metal chelators. Also the reactivation of saccharifying amylase was inhibited by sulfhydryl reagents, although the native enzyme was quite insensitive to the chemicals. In the acid-inactivation and reactivation process, a reversible change in the ultraviolet absorption spectra of the enzymes was observed, and some discussion of the implication was presented.

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A biotinless mutant (K-681-UV-134) accumulated a large amount of desthiobiotin and an unknown biotin-vitamer in the culture medium.
The parent strain (K-681) of this mutant isolated from soil was identified as Bacillus cereus.
The unknown vitamer was accumulated at the early stage of the incubation in com-parison with desthiobiotin.
The unknown vitamer was purified by the paper- and column-chromatographic methods from the culture filtrate. The purified vitamer gave a single spot when spraying with the ninhydrin reagent after paper chromatographing and its RF values in several solvent systems were identical with those of authentic 7-keto-8-aminopelargonic acid.

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Contents of arginine, methionine, histidine, phenylalanine, tryptophan and tyrosine were measured in the “Extract” and the “Fibrous” proteins obtained by urea fractionation from the skeletal muscle of rats fed a normal, a tryptophan-free and a protein-free diets for 30 days respectively. The ratios of the “Extract” to the “Fibrous” proteins were remarkably different in the muscles of the different dietary groups. Significant differences, were observed in the amino acid compositions of the protein fractions between the normal and both deficient groups showing the presence of the different dietary effects on the constituent proteins of the muscle.

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A quantitative fractionation method of muscle protein was presented. Muscles from the adult rats fed a normal, a tryptophan-free and a protein-free diets separately for 4 weeks were fractionated by this method. The effects on the composition of the muscle protein fractions were different between the tryptophan-free and the protein-free diets. The decreases of non-protein nitrogen and sarcoplasmic protein by both deficient diets were greater than that of total muscle nitrogen, whereas those of actin, myosin and stroma were smaller. This shows the presence of the different dietary effects on the constituent proteins of muscle.

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An acid protease of Rhizopus chinensis was purified by sequential chromatographies on columns of Duolite A-2, Sephadex G-100 and CM-cellulose, and crystallized from aqueous acetone solution. The preparation was shown to be monodisperse on column chromatography of ion-exchange sephadex and on ultracentrifugal analysis. The enzyme was most active at pH values between 2.9 and 3.3 and was stable over the range of pH 2.8 to 6.5. The protease was markedly inactivated by ferric ions and sodium lauryl sulfate, whereas it was affected by neither sulfhydryl reagents nor metal-chelating agents. In milk-clotting activity, the acid protease was shown to be one of the most potent enzymes among those of fungal origin. Substrate specificity experiments on several synthetic peptides indicated that the peptide bonds susceptible to the action of the enzyme were mainly those involving amino group of aromatic amino acids.

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Substrate specificity of the crystalline neutral protease of B. amylosacchariticus was investigated using the B-chain of oxidized beef insulin as the substrate, and the results were compared with those of proteases obtained from other strains of Bacillus subtilis. The neutral protease split the B-chain at eleven sites of the peptide linkages, indicating the narrow specificity as compared with subtilopeptidase A. The results also indicated that the peptide bonds susceptible to the action of the neutral protease were mainly those involving amino group of hydrophobic amino acids and tyrosine, with a few exception. The enzyme showed potent activities in casein digestion at near neutrality and in milk clotting at pH 5.6, whereas it was completely inert on esters and keratin, and only slightly active toward elastin.

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A general review of the acetic acid bacteria belonging to the intermediate type was accomplished physiologically, biochemically and morphologically. Conclusively, it was clarified that these were clearly a specific group and different from both Acetobacter and Gluconobacter. These were intermediate between lactaphilic and glycophilic, besides, on the carbohydrate oxidizability, these were intermediate between Acetobacter and Gluconobacter as mentioned previously.¹⁾ These showed the same result as Acetobacter on the vitamin requirement for the growth, but were closely related to Gluconobacter on the carbohydrate availability. And on the oxidative activity for amino acid, accompanying the deamination, these were also clearly distinguished from both Acetobacter and Gluconobacter, particularly these oxidized strongly L-serine. Differing from the observations by other investigators, these showed single flagellation, with the exception of multi-polar, but never multi-peritrichous.

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α- and γ-L-Glutamyl dipeptides of L-β-phenyl-β-alanine are synthesized for the first time from L-glutamic acid and L-β-phenyl-β-alanine. In addition, the preparations and the properties of new intermediates, that is, L-β-phenyl-β-alanine benzylester p-toluenesul-fonate and the N-carbobenzyloxy-α- and γ-dipeptide benzylesters, are described. Further proof of the structure previously proposed for the naturally occurring peptide is obtained by a critical comparison of the isolated and synthetic materials by various physical and chemical methods.

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Weanling male rats of Wistar strain were fed ad libitum 7 or 8% casein-α-starch diet supplemented with 0.3% DL-methionine with (+Thr) or without (-Thr) added 0.36% DL-threonine for 12 days. Urine was collected 3 times for 3 days each at one-day interval. The urine sample was analysed for allantoin, urea and total N.
There was no difference between the values of growth rate, liver and carcass fat con-tent, protein efficiency ratio and % N retention of -Thr and +Thr groups, whereas urea excretions of -Thr groups were significantly higher (over 2 times) than those of +Thr and allantoin excretions were consistently lower in the former when dietary protein level was 8%.
These results suggest again that urinary urea may be a most sensitive external indicator for detecting the differential changes in body protein metabolism, which are caused by slight modification of dietary amino acid composition.

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