In the latest work, a method to determine calorimetrically the α-glucosidic linkage contents in starches was introduced.
The present work refers to the application of this method to the determination of the α-1, 4 glucosidic linkage content in two kinds of sweet potato starch (i.e., Norin-1 and Okinawa-100) isolated at the two different stages of development.
It has been found that the sample isolated on October 31 (1953) had a larger value for α-1, 4 glucosidic linkage content than the sample isolated on August 6 (1953) for both the two sweet potato starches.
Combined with the amperometric titration method the increase in α-1, 4 glucosidic linkage content has been found to be due to both the increases in amylose content and in average unit chain length of amylopectin component.

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1. Effects of amino acids content, pH, fermentation temperature, aeration of the fermenting medium and yeast strain on the formation of higher alcohols were studied.
2. The contents of amino acids and ammonium affected largely the composition of higher alcohols formed, and are considered one of the most important factors making the different A/B ratio between a grain-madealcoholic beverage and a fruit-made-alcoholic beverage.
3. Fermentation temperature, aeration of the fermenting medium and yeast strain used affect the composition of higher alcohols formed.

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The arrangement of β-1, 3 linkage in previously reported F-1 β-glucan prepared from the endosperm of naked barley has been examined using the Smith degradation method. The fact that degradative products consists mainly of 2-0-β-D-glucopyranosyl-D-erythritol and erythritol with a small amount of 2-0-β-laminaribiosyl-D-erythritol, indicates that the arrangement of the β-1, 3 linkage in F-1 β-glucan is relatively regular.

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The purified 7S protein from soybean casein fraction contained approximately 4% mannose per protein. Mannose in the protein com-bined tightly with the protein and seemed to make a protein-carbohydrate complex as a glycoprotein. Hexosamine which was con-tained in the 7S protein was about 1.2% per protein.

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A neutral protease of Bacillus subtilis var. amylosacchariticus was purified and crystallized by sequential chromatography on columns of Duolite A-2 anion-exchange resin, CM-cellulose and DEAE-sephadex A-50. The crystalline preparation was chromatographically homo-geneous and confirmed to be monodispersive by physicochemical criteria. The enzyme was most active at near pH 7 against casein and stabilized by calcium salts. Some metal-chelating agents and metal ions such as Hg⁺⁺, Pb⁺⁺, Cu⁺⁺ and Fe⁺⁺⁺ markedly inactivated the enzyme, whereas diisopropyl phosphorofluoridate, sulfhydryl reagents and protease inhibitor of potato did not affect the activity. The neutral protease obtained here was rather stable as compared with the neutral protease ever reported and was able to be freeze-dried without any appreciable lose in enzyme activity.

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So called ambreinolal (IV), ^* a component of ambergris, was first synthesized by CrO₃ oxidation of ambreinolol (III)^* which was obtained from ambreinolide (II) by reduction with LiA1H₄. Ambreinolol (III) was converted to the C₁₇-saturated oxide (VII) in a good yield through the monotosylate (VIII) by treatment with p-toluenesulfonyl chloride in pyridine.

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Ambrein (I), a major constituent of ambergris, was easily converted to ambrein-tetrahydropyranylether (II), of which thermal decomposition gave back ambrein (I). The tetrahydropyranylether (II) was oxidized to ambreinolal-tetrahydropyranylether (V) in two steps. Ambreinolal-tetrahydropyranylether (V) was synthesized from ambreinolol (VII) in four steps and converted to the C₁₇-unsaturated oxide (VI) on heating.

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A pronounced increase of the activity of phenylalanine deaminase and tyrase during the lignification of bamboo shoots was observed. With progressing maturation from the basal part to the upper part of immature bamboos the pattern of the activity of the enzymes moved toward the upper part of the tissues, where the most active lignification was taking place, and the amount of cinnamic acid derivatives in the tissues was found to be in good accordance with the activity of the enzymes. L-Phenylalanine-G-¹⁴C and L-tyrosine-G-¹⁴C were both well incorporated into the lignin of bamboos. These results indicate that phenylalanine deaminase and tyrase are synthesized progressively just before the lignification of the bamboos and by the enzymes L-phenylalanine and L-tyrosine are deaminated to cinnamic acid derivatives and incorporated into lignin.

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1. Brev. lactofermentum rapidly removed biotin from culture medium. The amounts taken up exceeded the quantities required for maximal growth. Two significant levels of cellular biotin were observed in this micro-organism. They are a minimum level most adequat to the accumulation of L-glutamic acid (approximately 0.5μg/g), and a saturation level (approximately 20μg/g)
2. Biotin stored in cells was metabolically available, if the cells were subsequently placed in a medium lacking in biotin. In the subse-quent culture, the biotin level of cells was gradually reduced to the minimum level (0.5μg/g), as the cells multiplied, and then the accumulation of L-glutamic acid began.
3. The addition of Tween 60 in the subse-quent culture impaired the relation between the level of cellular biotin and the accumula-tion of L-glutamic acid. Since Tween 60 was incapable of preventing biotin from being taken up, it hindered the action of the absorbed biotin. Therefore, even biotin-saturated cells accumulated L-glutamic acid in the presence of Tween 60.
4. Saturated fatty acids with fourteen to eighteen carbons as well as Tween 60 had partial inhibitory effect on the subsequent growth of the biotin-saturated cells.
5. The bioautograms of the acid hy-drolysates of the cells exhibited a characteristic peak near to RF 0.85 and were identical with that of authentic d-biotin, using L. arabinosus as an assay organism. In addition, the growth I of Brev. lactofermentum was supported by the hydrolysate of the cells with minimum biotin, s and the combinability of avidin with the r biotin in the hydrolysate was observed in the f culture of this microorganism. From these observations, the existence of biotin was t evidently demonstrated in the cells.

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Alkaline degradation of Aurasperone A, C₃₂H₂₆O₁₀, gave a binaphthyl (IIa), m. p. 255°C and acetone. (Ila) afforded a tetraacetate (IIb), C₃₂H₃₀O₁₂ m. p. 219°C and_??_tetramethyl ether (IId), C₂₈H₃₀O₈, m. p. 188°C. These facts along with the NMR spectra of aura-sperone A and (IIb) confirm that aurasperone A is a dimeric 2-methyl-5-hydroxy-6, 8-dimethoxy-4H-naphtho [2, 3-b] pyran-4-one with asymmetric C-C linkage (7-10' or 9-10'). The ether (IId) is not identical with 1, 1', 3, 3', 6, 6', 8, 8'-octamethoxy-4, 4'-binaphthyl. Thus, it follows that (IId) is a 2, 4'-binaphthyl and hence aurasperone A is 2, 2'-dimethyl-5, 5'-dihydroxy-6, 6', 8, 8'-tetrahydroxy-7, 10'-bi [4H-naphtho [2, 3-b] pyran-4-one] (I).

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In the mustard paste, sinalbin is hydrolyzed by myrosinase to p-hydroxybenzyl isothiocyanate (I), sinapine acid sulfate and glucose. It was found that the three decomposition products were formed from sinalbin, and two of them were isolated from the mustard paste and identified as p-hydroxybenzyl alcohol (II) and di-(p-hydroxybenzyl)-disulfide (IV), respectively. II was_??_major product and IV was a minor product.

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1. Two fractions containing milk β₂A-globulin were prepared from human milk, and milk β₂A-globulin was isolated by re-chromatography of the fractions on DEAE-cellulose column.
2. Chemical composition of the final preparation of milk β₂A-globulin was as follows: nitrogen 11.01%, phosphorus 0.13%, hexose (galactose+mannose) 3.43%, hexosamine (glucosamine) 3.74%, fucose 2.72% and sialic acid 3.22%.
3. The final preparation of milk β2A-globulin was pure immunoelectrophoretically and electrophoretically with an electrophoretic mobility of -2.8×10^-5 cm² volt^-1 sec^-1 in a veronal buffer (pH 8.5, ionic strength 0.1) at 0.1 and an isoelectric point at pH 5.8.
4. By sedimentation experiments, it appeared to be homogeneous in a phosphate buffer (pH 7.0, ionine strength 0.1). The sedimentation coefficient extraporated to zero concentration was 5.14S.

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Adenine-auxotrophic mutant of Bacillus licheniformis formed considerable amount of guanosine from guanine. The guanosine formation was stimulated by the addition of penicillin to the growing cells and by the presence of uridine in the crude extract. The crude extract preserved for long time showed the changes of the enzyme actions for added guanine.

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3-Methylthiopropylamine hydrochloride was prepared from D, L-methionine and aceto-phenone in 90_??_92% yield by heating. Methionine sulfone was decarboxylated to γ-aminopropylmethyl sulfone, which migrated at the same rate as the authentic sample obtained from 3-methylthiopropylamine by hydrogen peroxide treatment. S-Alkylcysteines (R=methyl, ethyl, n-propyl, n-butyl and n-amyl) were also decarboxylated to give a product which showed new spots of 2-alkylthioethylamine with higher R_F values than those of the corresponding amino acids.

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