A corrinoid, formed predominantly in the cells of Streptomyces olivaceus 605 grown aerobically on a glucose-lactose medium, was identical with 5, 6-dimethylbenzimidazolyl-cobamide coenzyme (DBC coenzyme) by paper chromatography, paper ionophoresis, absorption spectrophotometry, assay of the coenzyme activity in diol dehydratase system and other tests.
Immediately after the maximal growth, the corrinoid was excreted into the cultural filtrate and converted to various unidentified forms of corrinoids.

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In a medium containing glycerol as u carbon source, Streptomyces olivaceus 605 accumulated under mild aeration a large amount of porphyrin in the culture filtrate. Identity of methyl ester of the porphrin with coproporphyrin III methyl ester was confirmed by UV-, IR- and NMR- spectroscopy. Under the cultural conditions favarable for production of corrinoid, the accumulation of coproporphyrin III markedly decreased.

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The high yield strain was isolated by the direct selection process using the naphtha-lene plate prepared by a new technique. The highest conversion rate of 94 weight per cent was obtained by studying the relationship among factors which affect the salicylate accumulation and degradation pattern. The almost complete conversion seems to be a result of inactivity of the salicylate oxidation enzyme until the exhaustion of naphthalene. The authors found it possible for the high-concentrated accumulation to neutralize the acidity of the accumulated salicylic acid indirectly by the addition of urea, instead of alkali or high-concentrated phosphate.

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Comparative study of acetaldehyde, furfural and 5-hydroxymethyl furfural from cellu-loses which differed in crystallinity was made by pyrolytic gas chromatography.
Pyrolysis of tobacco cellulose at 200-300°C resulted in rapid increase in the yields of furfurals from the amorphous regions in comparison with that from the crystalline regions. At 500°C, however, acetaldehyde was obtained in higher yields from microcrystalline cellulose than that from tobacco cellulose under the same condition.
In thermogravimetric analysis, the threshold temperature for the pyrolysis of tobacco cellulose was lower than that of microcrystylline cellulose. These results showed that the yields of the volatile compounds from pyrolysis of cellulose depended on temperature and crystallinity.

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The occurrence of lysogeny and bacteriocinogeny was systematically investigated in 106 strains of Clostridium species (non-pathogenic and mostly acetone-butanol- or isopropanol-butanol-producing) by cross-testing all the strains against each other. Consequently, it was found that 4 strains were lysogenic and other 18 strains bacteriocinogenic, and that all the strains were sensitive to one or more of bacteriocins and 15 strains of them were sensitive to the phages as well as bacteriocins.
The four temperate phages isolated were indistinguishable from each other in their host ranges, serological properties and other characteristics tested, and named as KT.
Grouping of the bacteriocins on the basis of their activity spectra and their specificity against bacteriocin-resistant mutants showed that 18 bacteriocins fell into 5 groups. The bacteriocins were named as clostocin, and groups of clostocin were designated as A, B, C, D and E, respectively.
There was cross-resistance between KT-phage and clostocin A, suggesting a common receptor. There were no correlations between the KT-phage or clostocins and the HM-phages of Cl. saccharoperbutylaeetonicum.

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Lipids and pigments of photosynthetic bacteria, Rhodospirillum rubrum and Rhodop-seudomonas capsulatus were examined. Common and prominent lipids in both bacteria were phosphatidyl ethanolamine and phosphatidyl glycerol. Rhodospirillum rubrum contained a special lipid containing ornithine. Their component fatty acids were straight chain saturated and monoenoic acids. No glycolipids were found in both bacteria. Ubiquinone-50 was detected in large amounts in both bacteria, and a new quinone and rhodoquinone were found in Rhodospirillum rubrum. The major carotenoids were spirilloxanthin, lycopene, and probably rhodopin. The results were compared with those of spinach and Anacystis, and discussed.

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The amount of isovaleraldehyde produced by the reaction of L-leucine with various carbonyl compounds including degradation products of sugar was determined, and relative reactivities of these carbonyl compounds in Strecker degradation were compared. The relatively high reactivity of DL-glyceraldehyde in Strecker degradation was considered to be partly due to the formation of pyruvaldehyde which was isolated as its bis-2, 4-dinitrophenyl-hydrazone from the reaction mixture of L-leucine and DL-glyceraldehyde. Formation mechanism of pyruvaldehyde was also proposed.

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Elemental sulfur was metabolized in the colloidal state by cell-free extracts of T. thiooxidans. The activity was found in the soluble fraction (in the supernatant of centrifu-gation at 130, 000×g for 1hr). The reaction products were sulfide and thiosulfate. p-Chloromercuribenzoate, acetate monoiodide and potassium cyanide inhibited the reaction.

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In order to elucidate the significance of amino groups as active groups of lysozyme, egg white lysozyme was acetylated with acetic anhydride. The acetylated lysozyme was fractionated by CM-cellulose column chromatography. All acetylated lysozymes fraction-ated exhibited 120% relative activity toward glycol chitin at pH 5.6, while the optimum pH shifted to the alkaline side by 0.5 pH units. Trinitrophenylated lysozyme, which was derived from acetylated lysozyme with 1.1 free amino groups per mole and which contained no amino group itself, retained 75% relative activity toward glycol chitin. These results indicate that the amino groups in the lysozyme molecule are not involved in the active site.
Acetylated lysozyme behaved the same as the untreated enzyme except the suscepti-bility to proteolytic digestion.

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Acetylated lysozyme retained full activity toward glycol chitin. However, lytic activity toward cells of Micrococcus lysodeikticus in neutral media decreased in proportion to the number of amino groups acetylated and its optimum pH shifted to the acid side with increase in the number of acetyl groups introduced. In the acid region below the optimum pH, the lytic activity was the same as that of untreated lysozyme. Very similar results were obtained using cell wall suspension.
The first step in lysis of bacterial cells by lysozyme seems to be an interaction between the positive charges of lysozyme and the negative charges on the surface of the bacterial cells. Acetylation of the free amino groups of lysozyme results in a diminution in the numbers of positive charges, causing a decrease in the interaction at neutral pH values. The second step of lysis is hydrolysis of the β-1, 4-glucosaminide linkage in the polysac-charide of the cell wall. The last step is dissolution of the damaged cell wall.

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Nonexacting purineless mutants were isolated from an inosine-forming adenine auxo-troph of Bacillus pumilus. Some of them accumulated Bratton-Marshall reaction-positive material in their culture fluid. The product was isolated in crystalline form and identified with 5(4)-amino-4(5)-imidazolecarboxamide riboside (AICA-Riboside).
AICA-Riboside accumulated by the nonexacting purineless mutants was less than inosine accumulated by their parent adenine auxotroph.
A number of mutants that require adenine specifically were isolated from AICA-Riboside-forming purineless mutants. More than half of them accumulated a large amount of AICA-Riboside as compared with their parents, nonexacting purine auxotrophs. The rest of adenine-requiring mutants from purineless mutants lost the ability to accumu-late AICA-Riboside.
The effect of hypoxanthine on the accumulation of ACIA-Riboside by these auxotrophs was also examined.

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In order to isolate and purify glutelin from rice endosperm, Kondo's method had been widely employed. However, we found that this method was not sufficient to prepare pure glutelin for structural studies, because glutelin prepared by this method would be easily contaminated with some impurities such as carbohydrates, nucleic acids and alkali-denatured albumin and globulin. Then we introduced a new method, which essentially involved the simultaneous extraction of impurities and precipitation of glutelin at pH 10.0 in the presence of sodium chloride. The purified glutelin by this new method had high nitrogen-content, 17.9%, and very low contents of phosphorus, pentose (nucleic acid) and hexose. The N-terminal analysis by FDNB method also revealed that the prepara-tion was chemically pure and glycine was the only one detectable terminus of glutelin.

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The composed having the proposed structure for auxin b lactone (XVIII) was synthe-sized by formic acid hydrolysis of 4-ethoxy-6-(3, 5-di-sec-butyl-l-cyclopenten-l-yl)-5, 6-dihydro-2-pyrone (XVII) which was, in turn, prepared by the Reformatsky reaction of 3, 5-di-sec-butyl-1-cyclopentenealdehyde (XVI) with ethyl γ-bromo-, β-ethoxycrotonate.

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Increased levels of maleate cis-trans isomerase in Alcaligenes faecalis IB-14 were induced by malonate analogues such as tartronate, keto-malonate and ethyl-malonate. Similarly in the case of malonate, those analogues were not served as carbon sources for the cell growth, but they were more effective as inducer than maleate, the normal inducer of the enzyme.
The induced synthesis of the enzyme was markedly repressed in the presence of various carbon sources, e.g. oxalacetate, D- and L-malates, fumarate and succinate. More than 90 per cent of the enzyme formation was inhibited when 10^-1 M of oxalacetate or DL-malate was present in malonate medium. The repression of the enzyme synthesis by those dicarboxylic acids was always associated with remarkable promotion of the cell growth.

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Physico chemical changes of ovalbumin illuminatied in the presence of methylene blue were examined. Solubility of ovalbumin was remarkably reduced, but its extents were varied with the value of pH, that of ionic strength and illumination time. Illumination brought about aggregation of protein molecules which was revealed on the ultra centrifugal patterns. Electrophoretical patterns showed that three peaks characteristic of native ovalbumin went into one peak after 24 hr and into two peaks after 48hr. After an illumination for 6 hr, titration curves showed that bound protons decreased below pH 8.0 and increased over pH 8.0. The spectra of illuminated ovalbumin were displaced upward and the absorption maximum shifted toward the longer region of wave length.

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A screening method for the antibiotics capable of inhibiting synthesis of nucleic acid in bacterial cells or mammalian tumor cells was investigated. The DNA and RNA syn-theses in Bacillus subtilis 168 thymine-, indole- were studied by the assay of incorporations of ³H-thymine and ¹⁴C-uracil into the cells, respectively. With known antibiotics against nucleic acid synthesis, the adequacy of the method was examined, and the result proved that this method is more sensitive and specific than the conventional assay methods.
It was found as a new fact that cellocidin is a potent and specific inhibitor to the thymine incorporation into DNA.
By an almost similar procedure, an inhibitory effect of several antibiotics on the incorporations of ³H-thymidine and ¹⁴C-uridine into Ehrlich ascites carcinoma cells was also studied.

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Some general properties of the acid-stable dextrinizing amylase of black Aspergillus were investigated comparing with those of Taka-amylase A. The mode of action on starch of this amylase was quite similar to that of Taka-amylase A. Saccharifying degree at red point in starch-iodine color reaction was 5.1% and the limit of starch saccharification was a little over 40 per cent calculated as glucose with both amylases. Maltase activity was absent. Degradation products in the course of starch hydrolysis were also quite similar and they mutarotated downward. So this amylase was decided to be α-type. Thermal stability of the acid-stable α-amylase was higher than that of Taka-amylase A. Its acid stability was much higher than that of Taka-amylase A. Taka-amylase A was inactivated completely at pH 2.2, 37°C, for 30min, but the acid-stable α-amylase retained 87% of its original activity.

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From the amylase preparation of black Aspergillus acid-stable α-amylase and acid-unstable α-amylase were separated by gel filtration on sephadex G-100 column. From the acid-unstable α-amylase fraction this enzyme was purified by fractionations with rivanol and acetone, and finally obtained as a homogeneous protein after gel filtration with sephadex G-50. Comparison of some general properties between the two α-amylases was carried out. Catalytic action was quite similar with both enzymes, but dextrinizing unit per mg enzyme protein of the acid-unstable α-amylase was about 5.6 times as large as that of the acid-stable a-amylase. The acid-unstable α-amylase was less heat-stable than the acid-stable a-amylase. Acid stability and pH-activity curve were compared with both a-amylases. High stability of the acid-stable α-amylase in acidic condition was observed, but, in alkaline range, it was more sensitive than the acid-unstable α-amylase.

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