Chcmical composition of the filamentous cells of Lactobacillus delbrueckii produced by vitamin B₁₂ deficient culture was studied. Protein and RNA contents per unit cell volume of the filamentous cells were nearly equal to those of normal cells, but the DNA content was much reduced. A cytoplast of the filamentous cell possessed about twice as large volume as that of the normal cell. A cytoplast of either filamentous or normal cell seems to contain the same amount of DNA. DNA level and menlbrane formation necessary for cell division rcmained as futurc problems.

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Transaminase reaction between L-lysine and α-ketoglutaric acid was found in the cell-free extracts of Flavobacterium fuscum, Fl. flavescens and Achromobacter liquidum. The transaminase in the extract of Fl. fuscum was partially purified and some properties were investigated. The formation of glutamic acid proceeded stoichiometrically with disappearance of the substrates by transamination. D-Lysine and pyruvic acid, phenylpyruvic acid or oxaloacetic acid could not participate in this reaction as an amino donor and an amino acceptor, respectively. The activity of the transaminase was inhibited by addition of penicillamine. As the keto analogue of L-lysine did not react with 2, 4-dinitrophenylhydrazine to form a hydrazone, but reacted with o-aminobenzaldehyde and p-dimethylaminobenzaldehyde to produce respectively unique color, it was suggested that the keto analogue was present in a form of a cyclic compound containing a piperidine ring.

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When phosphorothioates had the CH₃-O-P linkage, they reacted with pyridine and consequently the linkage was cut off. Phosphorothioates having other alkyl-O-P linkages did not react with pyridine in the same condition as the above. Namely, O, O-dimethyl phosphorochloridothioate reacted with pyridine and produced mainly methylchloride and an oily product whose experimental formula is (CH₃O) PSO^-N⁺C₅H₅, and one mole ratio of O, O-dimethyl-O-(4-nitrophenyl) phosphorothioate also reacted with two moles ratio of pyridine and produced di-(N-methyl pyridinium) salt of O-(4-nitrophenyl) phosphorothioic acid.

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The effects on the polymorphic crystallization of L-glutamic acid were examined of many substances including amino acids, inorganic salts, surface active agents, and sodium salt or hydrochloride of L-glutamic acid, when contained in the mother liquor.
The co-existence of amino acids, especially of L-aspartic acid, L-phenylalanine, L-tyrosine, L-lcucine and L-cystine contributed to the crystallization of L-glutamic acid in α-form, and these amino acid showed an inhibitory action on the transition of α-crystals as the solid phase in the aqueous solution, to β-crystals.
In the presence of a large amount of L-glutamate or the hydrochloride at the time of nucleation of L-glutamic acid, mostly β-crystals appeared even in the presence of the amino acids named above.

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The solubilities of L-glutamic acid crystals in α-form and β-form in water were determined, and the results were formulated as follows.
α-form: Log S=-0.377+0.0174t (t is from 0° to 30°C)
Log S=-0.328+0.0153t (t is from 30° to 70°C)
β-form: Log S=-0.461+0.0159t
The formula obtained for β-crystals showed a fair agreement with that reported by J. B. Dalton et al.

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Data for several additional instances of epoxidation by biological systems at isolated unsaturated sites on steroid structures are presented.
These systems include the bovine adrenal, Curvularia lunata and a Curvularia species. This reaction predictably occurred only in the presence of enzymes capable of introducing “axial” hydroxyl functions at saturated carbons of corresponding analogous structures. A discussion of the implication of these findings in terms of the mechanism of the enzymatic hydroxylation reaction is given.

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Neoilexonol, an unsaponifiable substance first isolated from the barks of Ilex goshiensis HAYATA and I. Buergeri MIQUEL (Aquifoliaceae), has now been proved to be formulated as 11-keto-α-amyrin, i. e., 11-oxours-12-en-3β-ol.

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Effects of alkali halides on radiation inactivation of Taks-amylase A were investigated in connection with their synergistic action to the radiation inactivation of microorganisms. Effective concentrations of these halides in protection against irradiation inactivation of this enzyme were well corresponded to that observed in the synergistic action to microorganisms. Removal of dissolved oxygen from halide solutions decreased their protective effect. Irradiated alkali halide solutions of relatively higher concentrations exhibited the inactivating action to this enzyme, and various types of addition effects of halogens and halogenoxyacids were observed with or without irradiation. Sodium nitrite showed effective protection even with higher radiation doses, and the heavy metal cations, Cu⁺⁺ and Fe⁺⁺⁺, also gave a protective action in low concentrations. From these observations, the possible interpretation on the mode of protection of alkali halides was attempted.

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To confirm the location of the lactone ring at ring A of gibberellin A₃, selenium dehydrogenation experiments were conducted in various ways, The results thus obtained and NMR spectrum studies rather support structure (III).

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On the catalytic hydrogenation of gibberellin A₃, the lactone ring was hydrogenized accompanying the double bond migration to C-10-C-11. The structures of two hydrogenolysis products thus obtained are discussed along with their acid-catalyzed relactonization. Subsequent dehydration of secondary hydroxyl groups at C-2 of these products gave unexpected aromatized compounds, the structures of which are also discussed.

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