It was found that the AMP phosphorylating activity of Candida sp. N-25-2 (a hydrocarbon assimilating yeast) was affected extremely by the liquid volume of cultural medium and the concentration of inorganic salts in medium. The yeast cells having no fermentative activity showed a strong activity of AMP phosphorylation when they were cultured under relative anaerobic conditions. It was observed that the glucose consumption of yeast cells was promoted by the addition of Mg⁺² ion and AMP into the reaction system, and that the AMP phosphorylation was promoted in the presence of F-1, 6-DP or phosphaenolpyruvate.
The cells of Candida sp. N-25-2 grown on glucose medium had a remarkable fermentative activity, while the cells grown on acetate or ethanol medium had a weak activity. On the other hand, it was found that the cells grown at strong aeration on glucose medium were able to produce remarkably the phosphorylated substances from mononucleotides, when F-1, 6-DP was added as a phosphate donor. Similar phenomenon was observed in case of the cells grown on the carbon sources such as acetate, ethanol and hydrocarbon.

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(±)-trans-Allethrin-(Z)-ol (IV), (±)-trans-allethrin-(Z)-al (V) and (±)-trans-allethrin-(Z)-
acid (VI), the minor components of allethrin metabolites in the insect body, were synthesized. The toxicities of newly synthesized allethrin derivatives (IV, V, VI) and of (±)-trans-allethrin-(E)-acid (Xc) to houseflies (Musca domestica L.) were examined by the injection method. And
their low toxicities seem to support the hypothesis that oxidation at the isobutenyl side chain
of the acid moiety of the allethrin molecule is a detoxication process in the insect body.

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A new metabolite, cotylenol, has been isolated from the culture filtrate of a fungal strain, 501-7w. Production and characterization of cotylenol are described. The chemical relationship between cotylenol and cotylenin A has been elucidated.

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From a consideration of the structure-activity relationships, nineteen 2- or 4-thiazolylmethyl cyclopropanecarboxylates, including three benzyl-thiazolylmethyl chrysanthemates (IVf, Xb and Xc), were prepared from thioamides and α-haloketones or α-haloaldehydes and examined for insecticidal activity against houseflies. All those with benzyl substitutions on the thiazole ring were ineffective, as were the other substituents. Only 4, 5, 6, 7-tetrahydrobenzothiazolylmethyl chrysanthemate and 2, 2, 3, 3-tetramethylcyclopropanecarboxylate (Xf and XIf) possessed about the same order of activity as allethrin, and their activities were 0.61 and 1.56μg/fly respectively.

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1. The oxidation of methanol to carbon dioxide by Candida N-16 grown on methanol was investigated. The presence of enzymes which catalyze the following reaction was found in the cell-free extract of the yeast employed; CH₃OH→HCHO→HCOOH→CO₂. 2. Methanol was oxidized to formaldehyde by an alcohol oxidase. The reaction was as follows; CH₃OH+O₂→HCHO+H₂O₂. The alcohol oxidase was crystallized after purification by ammonium sulfate-precipitation and column chromatography using DEAE-Sephadex A-50. A prosthetic group of the enzyme was proved to be FAD. The enzyme possessed a broad specificity for alcohols such as methanol, ethanol, n-propanol, n-butanol and n-amylalcohol. The enzyme was inducibly formed only by the addition of methanol. 3. The oxidation of formaldehyde to formate was catalyzed by a NAD-linked dehydrogenase dependent on GSH. 4. Formate was oxidized by a NAD-linked dehydrogenase. 5. Catalase was also found in the extract, and methanol was chemically oxidized by the reaction of catalase and hydrogen peroxide which was generated by the alcohol oxidase system. 6. The oxidation pathway from methanol to carbon dioxide was also found in other methanol-utilizing yeasts such as Candida N-17, Saccharomyces H-1 and Torulopsis M-1.

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A species of Erwinia was found to produce no other pectolytic enzyme than the two transeliminases of exo-types, namely, an oligogalacturonide transeliminase and an exopectic acid transeliminase. Of the two enzymes, the exopectic acid transeliminase was isolated and its properties were investigated. The results are as follows: (1) Pectic acids having an unsaturated galacturonic acid residue at the non-reducing end of the molecule are susceptible but oxidized or reduced pectic acids resistant to the enzyme action. (2) The enzyme has no activity toward pectinic acid and polymethylpolygalacturonate methyl glycoside. The limit of the enzymatic degradation for citrus pectic acid is 43.8%. (3) The rate of the enzyme activity was maximal with tetragalacturonic acid and followed by acid-soluble pectic acid, acid-insoluble pectic acid, pectic acid and trigalacturonic acid. Unlike the oligogalacturonide transeliminases of Pseudomonas sp. (strain S2) and Erwinia aroideae, the present enzyme shows a considerably high activity toward pectic acids of high molecular weight. (4) The pH-activity curves vary with the buffer employed. (5) The enzyme is activated by Co²⁺ and Mn²⁺ but powerfully inhibited by Cu²⁺ and Hg²⁺. Ca²⁺ has no significant effect on the enzyme activity.

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1. Some of 5-methyltrypotophan (5MT)-resistant mutants derived from glutamateproducing bacteria such as Brevibacteriwn flavnm, Corynebacterimn acetoglutamicum and Micrococcus glutamicus produced a small amount of L-tryptophan, while tyrosine and phenylalanine auxotrophs of B. flavum did not.
2. 5-MT-resistant mutant derived from the auxotroph for tyrosine and phenylalanine produced 390mg/liter of L-tryptophan at most. A mutant resistant to a higher concentration of 5MT, which was derived from a tyrosine and phenylalanine auxotrophic mutant which was resistant to a low concentration of 5MT, produced 660mg/liter of L-tryptophan. Using this mutant, the effects of the concentrations of components of the culture medium on the L-tryptophan production were examined. The high concentration of L-tyrosine, but not L-phenylalanine, inhibited the L-tryptophan production. Using the improved culture medium, this strain produced 1.9g/liter of L-tryptophan.

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A vitamin B₁₂-dependent N⁵-methyltetrahydrofolate-homocysteine methyltransferase was found in cell-free extracts of Corynebacterium simplex ATCC 6946 grown aerobically in a medium containing hydrocarbon as a sole carbon source and the enzyme was partially purified. Absolute requirements for S-adenosylmethionine and an appropriate reducing system were observed for the transmethylation from N⁵-methyltetrahydrofolate. The same preparation catalyzed also the formation of methionine from homocysteine and methyl-B₁₂ under both aerobic and anaerobic conditions. The concentration of cobalt ion in the growth medium had a pronounced effect on the intracellular vitamin B₁₂ level and the activity of the vitamindependent methionine-synthesizing system in the bacterium. The relationship between the methionine synthesis and the methyl branched-chain fatty acid formation was discussed.

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Candida tropicalis pK 233 exhibited marked morphological changes depending upon carbon sources for growth. Although the yeast showed a typical yeast-like development when grown on glucose, the cells grown on hydrocarbon or ethanol were composed of a mixture of filamentous-form (F-cells) and yeast-form cells (Y-cells). The carbon chain lengths of n-alkanes tested as growth substrates had a significant influence on the ratio of F-cells to Y-cells. Electronmicroscopic observation revealed that a hypha was divided by septa into several cells.
Separation of Y-cells and F-cells was achieved by using a suitable filter cloth. F-cells gave a high Qo₂ value compared with Y-cells when hydrocarbon was used as oxidation substrate, even though there was little difference between the respiratory activities of these two cells measured with glucose.

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The acid coagulability of casein from 54 individual human milk samples and the variation of coagulability of their casein preparations by rennin were examined. The casein and whey protein preparations from individual human milk samples were also compared by polyacrylamide gel electrophoresis (PAE). Casein coagulated distinctly from 22 human milk samples when the pH was adjusted to 4.6 with acid, but it did not from other 32 samples. Twenty-two samples of casein preparations coagulated distinctly by rennin in the presence of calcium ions but 19 samples just became turbid. When the classification of human casein based on PAE pattern of major six bands was applied in our preparations, type A appeared most often and type C did least. Any regular relationship was not found between variation of the PAE pattern of casein preparations from individual human milk samples and that of acid coagulability or rennin coagulability.

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Occurrence of milk acid protease in bovine casein in addition to alkaline protease was found and purification of this enzyme was achieved. The enzyme had a pH optimum at 4.0 and was most stable at pH 3.5. The molecular weight of the enzyme was 36, 000 and no inhibition was observed by diisopropyl-fluorophosphate, EDTA etc. This enzyme is considered to be similar to cathepsin D.
Milk acid protease mainly hydrolyzed α_s-casein and similar change was observed in autolysis of casein at pH 5.5. It is suggested that milk acid protease may have some significance in cheese ripening.

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In order to investigate the mechanism of microbial growth at elevated temperatures, it was tried to isolate different thermophilic microorganisms from wide origins, such as soils, composts, manure piles and hot spring waters. As the result, 5 strains of extremely thermophilic bacteria, the maximum, the optimum and the minimum temperatures for growth of which were 80, 70_??_75, and 40°C, respectively, were isolated from Izu-Atagawa hot spring and Beppu hot springs. These bacteria were gram-negative, yellow-pigmented, non-motile and non-sporulating rods of 0.5_??_0.7μ in diameter and 2_??_5μ in length. They were heterotrophs requiring several amino acids (such as glutamate, aspartate, et al.) and vitamins (such as biotin, folic acid and p-aminobenzoic acid) and grew well at neutral to slight alkali pH. The content of GC pairs of DNAs from the 5 strains was 69_??_70%, and this seemed to be one of the highest values in bacteria so far known. Among the 5 strains, strain AT-62 was named as Thermus flavus sp. _??_ AT-62 from its morphological and physiological characteristics. Comparison between Thermus flavus and other extremely thermophilic bacteria as Thermos aquaticus and Flavobacterium thermophihum is described and discussed in reference to classification of extremely thermophilic bacteria.

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Pectolytic enzyme formation by whole cells of Erwinia aroideae was markedly stimulated when nalidixic acid was added to a culture medium. The activity of pectolytic enzyme was markedly stimulated by nalidixic acid when the activity was measured by the decrease of viscosity of pectin, while activities of both polygalacturonic acid traps-eliminase and polygal-acturonase which were measured respectively by the increase of optical density at 230nm and the liberation of aldehyde groups, were not stimulated. The analysis of pectolytic enzyme by carboxymethyl cellulose column chromatography indicated that there was a significant difference in the elution profiles between the pectolytic enzyme induced by nalidixic acid and that synthesized under normal conditions. Therefore, we conclude that two enzymes are distinct protein species.

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Fructose-1, 2-cyclic phosphates(F-1, 2-Ps) and fructose-2-phosphates(F-2-Ps) were synthesized according to the method of Pontis and Fischer and their properties toward acid hydrolysis were examined in detail. Fructopyranose-2-phosphate(Ep-2-P) showed exactly the same properties as those reported by Pontis and Fischer. On the other hand, a part of fructofuranose-2-phosphate(Ff-2-P) was converted into the acid-stable form during acid treatment and this substance increased progressively when the sample was stored at -20°C for a longer time. This acid-stable form resembled in its properties to the fructose phosphate obtained from UDP(2)-fructose by the action of nucleotide pyrophosphatase.
When treated with acid at room temperature, fructopyranose-1, 2-cyclic phosphate(Fp-1, 2-P) was almost completely hydrolyzed into fructose and inorganic phosphate, whereas only about 50% of fructofuranose-1, 2-cyclic phosphate(Ff-1, 2-P) was hydrolyzed into fructose and inorganic phosphate and the remainder was hydrolyzed into fructose-1-phosphate(F-1-P). On the other hand, when treated with acid at 100°C, 90% of both cyclic phosphates were hydrolyzed into F-1-P, and fructose and inorganic phosphate were formed only slightly.

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Extracellular pullulanase was purified and crystallized from the culture fluid of Aerobacter aerogenes. Pullulanase was purified by means of ammonium sulfate fraction, DEAE-cellulose column chromatography and Sephadex column chromatography. Crystalline pullulanase was formed when saturated ammonium sulfate solution was added to the purified enzyme solution. The crystalline enzyme appeared as colorless fine rods. On ultracentrifugation analysis, the enzyme showed a single sharp and symmetrical Schlieren peak. The sedimentation coefficient, s_{20, w} was 4.39S. Polyacrylamide gel electrophoresis at pH 8.4 gave a main band with two sub-bands and the molecular weight of the main enzyme was estimated to be 66, 000 from polyacrylamide gel electrophoresis and to be 58, 000 from sedimentation equilibrium. The optimum pH and temperature for the enzyme action were pH 6.5 and 50°C, respectively.

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The plant-growth inhibitory activities of a number of compounds related to the podolactones were determined using a pea-stem growth system. Some conclusions regarding the effects of structure on activity are presented.

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To investigate the operation of a succinate transport system in Escherichia coli, mutants defective in succinate metabolism were isolated. Although the metabolic blocks in the mutant cells were not complete, the succinate transport assays became possible.
Pyruvate, lactate or many other carbon sources stimulated succinate uptake, and the uptake was strongly inhibited by some electron transport inhibitors, uncouplers of oxidative phosphorylation and sulfhydryl reagents. The mutant strains accumulated succinate into the cells against a concentration gradient when suitable energy sources were supplied.
Presence of glucose in the medium strongly repressed the formation of the succinate transport system. The optimum pH for the succinate uptake was between 7.8 and 8.0.

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Several new 3, 4-methylenedioxyphenyl derivatives structurally related to the Cecropia juvenile hormones were synthesized to be tested as inhibitors for metamorphosis of the larvae silkworm of Bombvx mori L.

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An NAD-linked formaldehyde dehydrogenating enzyme was found in the cell-extract of Kloeckera sp. No. 2201, which utilized methanol as a sole source of carbon. The enzyme was inducibly formed in methanol-grown cells. This fact suggests that the enzyme may play a significant role in the methanol metabolism of this yeast. The enzyme was purified from a cell-extract by ammonium sulfate fractionation, column chromatographies on DEAE-cellulose and on hydroxylapatite, and Sephadex G-200 gel filtration. From an experiment with the purified enzyme, it was found that the enzyme specifically required reduced glutathione for activity, and was reactive toward methylglyoxal as well as formaldehyde. The enzyme catalyzed the following reaction:
Formaldehyde+NAD+H₂O→formic acid+NADH+H_??_ the enzyme was concluded to be a kind of formaldehyde dehydrogenase (formaldehyde: NAD oxidoreductase, EC 1. 2. 1. 1). Other properties of the enzyme were also investigated.

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In order to determine the limiting dispersion glutenin in concentrated guanidine hydrochloride, the behavior of glutenin was observed in different concentrations of guanidine hydrochloride. Increase of intrinsic viscosity and decrease of turbidity were observed with increasing concentrations of guanidine hydrochloride up to 6M and a limiting state was attained above 6M. The molecular weight determination also gave a limiting value above 6M. The values obtained were 850, 000 for one preparation and 640, 000 for another. While the turbidity and viscosity in 6.5M guanidine hydrochloride were constant in the pH region from 4 to 5.5, they increased slightly around pH 6 and decreased toward pH 7. The viscosity of glutenin around pH 7 was lower than that around pH 4, but the same molecular weight was obtained at pH 4.0 and 6.9.

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Lipid components of a glycolipid, formerly designated as spot A, from the cells of Selenomonas ruminantium were investigated. The basic structure of this material had been previously shown to be β-glucosaminyl-1, 6-glucosamine. The major component of O- and N-acyl side chains was β-OH C_13:0 acid when the cells were grown with added valerate. Approximately 85% of the total amide linked fatty acids was this compound. A considerable amount of C_13:2 acid was also present as a component of O-acyl fatty acids. When the cells were grown in a glucose medium containing caproate, the major fatty acid component of the spot A compound was β-OH myristic and β-OH C_13:0 acids. ¹⁴C-Valerate or ¹⁴C-eaproate, supplemented to the glucose medium, was incorporated into O- and N-acyl linked fatty acid moieties of the spot A compound. It was also shown that the spot A compound was the lipid A component of lipopolysaccharides of this organism.

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(±)-Sermundone (2), one of the hydroxyrotenoids, has been synthesized. Also a new cyclization method to dehydrorotenoids has been developed using alkali metal salts.

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The induction of metallic mercury-releasing enzyme (MMR-Enz) which catalyzes the reduction of mercurials to metallic mercury was studied. The formation of MMR-Enz was induced when the organism was grown with mercurials such as phenyl mercuric acetate (PMA), p-chloromercury benzoate (pCMB), sodium ethyl mercuric thiosalicylate (merzonin), mercuric chloride (MC) and metallic mercury, but it was not induced when grown with HgS or other metals such as Ag⁺, Gd²⁺, Cu²⁺, Fe²⁺, Co²⁺, Sn²⁺, etc. Cd²⁺ and Cu²⁺ were inhibitory for the formation of MMR-Enz. D-glucose: NAD oxidoreductase (EC 1. 1. 1. 47 GDH) or L-arabinose: NADP oxidoreductase (EC 1. 1. 1. 46 ADH) and cytochrome c-I (cyt. c-I) which were all involved in the decomposition of mercurials together with MMR-Enz were found in the crude extract regardless of mercurial addition. These results suggest that MMR-Enz plays a conclusive role on the decomposition reaction of mercurials.

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Acid hydrolysis of asterosaponin A afforded a crystalline 6-deoxyglucobiose, whose structure has been established as O-(6-deoxy-α-D-glucopyranosyl)-(1→4)-6-deoxy-n-glucose. This is the first isolation of a 6-deoxyglucobiose. Its formation as _??_ hydrolytic fragment of asterosaponin A suggests the presence of an α-1→4'-glycosidic linkage between the two 6-deoxy-D-glucose units in the saponin.

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Partial acid hydrolysis of asterosaponin A, a steroidal saponin, afforded two new disaccharides in addition to O-(6-deoxy-α-D-glucopyranosyl)-(1→4)-6-deoxy-D-glucose which has been characterized in the preceding paper.¹⁾ The formers were demonstrated as O-(6-deoxy-α-D-galactopyranosyl)-(1→4)-6-deoxy-D-glucose and O-(6-deoxy-α-D-galactopyranosyl)-(1→4)-6-deoxy-D-galactose, respectively.
Accordingly, the structure of carbohydrate moiety being composed of two moles each of 6-deoxyDo-galactose and 6-deoxy-D-glucose, was established as O-(6-deoxy-α-D-galactopy-ranosyl)-(1→4)-O-(6-deoxy-α-D-galactopyranosyl)-(1→4)-O-(6-deoxy-α-D-glucopyranosyl)-(1→4)-6-deoxy-D-glucose, which is attached to the steroidal aglycone through an O-acetal glycosidic linkage.

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Previous works have demonstrated that a computerized learning machine could be successfully applied to predicting the presence or absence of a certain microbial feature in a microorganism. To achieve the prediction, however, the presence or absence of many other features must be examined beforehand. This paper deals with the method for decreasing the number of characters that must be examined prior to the prediction. In the six instances studied, this number could be decreased from 93 to 11 in the most fortunate case and to 26 in the most unfortunate case, without causing deterioration of the prediction results.

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A neuroactive substance was isolated in colorless crystalline state from body fluid of silkworm larvae which had been poisoned with DDT. It increased a spontaneous activity on the isolated abdominal nerve cord of American cockroaches, and resembled to the Sternburg's unknwon neuroactive substance¹⁾, in some respects. This compound was, however, not aromatic amine but was identified as L-leucine by mass spectra, infrared absorption spectra, ultraviolet absorption spectra, and paper chromatography. Authentic L-leucine also showed a high neuroactivity.
Various kinds of other amino acids were also tested on the isolated nerve cord of cockroach, and they did not show any increase of spontaneous discharge except L-alanine, which appeared to have a weak neuroactivity.

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Nutritive value of 4 glycol esters, i.e. ethanediol diacetate, 1, 2-propanediol diacetate, 1, 3-butanediol diacetate and 1, 3-butanediol dioctylate, was estimated biologically by feeding the esters to growing chicks and rats. Energy in the esters taken by both chicks and rats was well utilized, though feed intake of the diets containing the esters at high level tended to decrease. Bitter taste of the esters was suspected to be related to low appetite. The acetates were somewhat volatile and released free acetic acid in the diet during storage. These properties of the acetates makes their use for dietary energy source difficult in practical condition.

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Monochlorotrifluoro-p-benzoquinone (CFQ) was used for investigating the state of the amino groups of acid-stable α-amylase and acid-unstable α-amylase. About half of the total amino groups in both enzyme molecules were reacted with the reagent. The unreactive amino groups seemed to exist in a different state from the reactive ones. Both enzymes whose amino groups were modified by CFQ still maintained the α-phenylmaltosidase activity in spite of losing or decreasing the amylase activity. These facts suggest that the amino groups of both enzymes were not in the active site but the modification of them caused steric hindrance.
The pH-stability of the acid-unstable α-amylase whose one or two amino groups were modified with succinic anhydride or 2, 4, 6-trinitrobenzene-1-sulfonate (TNBS) increased on the acidic side and decreased on the alkaline side, but further modification of them led to decrease the stability on both sides.

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To investigate the stereo-specificity and the genetic control of a succinate transport system, mutants of Escherichia coli defective in the transport of succinate were isolated. The mutants showed no detectable growth on fumarate and malate, as well as on succinate. All of the revertant strains from one of the transport defective mutants, T5, could grow either on succinate, fumarate or malate. The T5 cells accumulated only a trace amount of ¹⁴C-succinate or ¹⁴C-fumarate. These results indicated that at least succinate, fumarate, and malate were transported by the system involving the same component. From the competition experiments, it was suggested that oxalacetate was also transported by the same system. A partial participation of this system for the transport of aspartate was suggested.

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Four proteins (F-IA, B, F-IIA & F-IIB), having myrosinase activity, were separated and purified from mustard powder. Each enzyme was shown to be homogeneous chromatographically, ultracentrifugally and Disc electrophoretically. Molecular weights obtained by gel-filtration and sedimentation equilibrium were 153, 000 (F-IA, F-I B & F-IIA) and 125, 000 (F-IIB). Sedimentation coefficients were 6.8S (F-IA, B & F-IIA) and 5.8S (F-11B). Stokes radius (Å), diffusion coefficient (cm²/sec) and frictional ratio (f/fo) were 47, 4.28×10^-7 and 1.33 (F-IA, B & F-III), and 43, 4.67×10^-7 and 1.29 (FIIB), respectively. Isoelectric points were pH 4.6 (F-IA, B & F-IIA) and pH 4.8 (F-IIA). The enzymes were glycoprotein with 9_??_22% carbohydrate. Amino acid composition of F-IA, Band F-IIA were very similar, but in case of F-IIB, glutamic acid, arginine and methionine contents were higher and aspartic acid and histidine contents were lower than others. The molecular weights estimated from SDS-polyacrylamide gel electrophoresis were 40, 000 (F-IA, B & F-IIA) and 30, 000 (F-IIB), respectively, and hence the enzymes are considered to have at least 4 subunits. From these results, it may be confirmed that F-IA, B & F-IIA have striking resemblances and only F-IIB is rather different.

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Some α-methylene-γ-butyrolactones and congeners were synthesized and their growth inhibitory activities were assayed on rice seedlings and Avena coleoptile sections. In the latter bioassay, the inhibitory activities of the synthetic α-methylene-γ-lactones were comparable to those of heliangine and pyrethrosin, the natural inhibitors possessing α-methylene-γ-lactone moiety.

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Aurasperone C (III) shows properties closely related to those of aurasperone B (II) and gave dianhydro compound (V) on hydrochloric acid treatment. Partial methylation of (V) with methyl iodide afforded a monomethyl ether identical with aurasperone A (I).
NMR studies, including solvent induced methoxyl shifts, indicate the structure of (III) to be 2, 2'-dimethyl-2, 2', 5, 5'-, 8-pentahydroxy-6, 6', 8-trimethoxy-7, 10'-bi [2, 3-dihydro-4H-naphtho [2, 3b] pyran-4-one], in which the 8-methoxyl of aurasperone B is replaced by a hydroxyl group.

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Stereochemistry at C-16 of dihydrogibberellin A₁ methyl ester (methyl tetrahydrogib-berellate, III) and its 16-epimer was elucidated. NMR nalysis employing a shift reagent, Eu(thd)₃ or Eu(fod)₃, was found to be very effective for settling this stereochemical problem.

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The tryptophanase activity which synthesizes L-tryptophan from pyruvate, ammonia and indole, was found to be widely distributed in cells of bacteria belonging to Enterobacteriaceae, such genera as Escherichia, Kluyvera, Enterobacter, Erwinia and Proteus. With the cells of Proteus rettceri, equilibrium of the elimination reaction of L-tryptophan in the presence of high concentration of ammonia was studied. It was found that the equilibrium inclines toward the synthetic state.
When 5-hydroxy- and 5-methyl-indole were substituted for indole, 5-hydroxy- and 5methyl-L-tryptophan, respectively, were synthesized. The synthesis of L-tryptophan was also observed with indole and various amino acids, S-methyl-L-cysteine, S-ethyl-L-cysteine, Lcysteine, 5-fluoro-DL-tryptophan, or oxalacetic acid.

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A piscicidal constituent, C₃₂H₄₂O₈, was isolated from Sapium japonicum. On the basis
of the chemical and spectral studies, the structure of the piscicidal constituent was shown to
be 1a, 12-O-n-deca-2, 4, 6-trienoyl-phorbol-(13)-acetate.

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A total synthesis of some kaurane derivatives with an oxygen function in ring A was accomplished. They are potential intermediates for the synthesis of highly oxygenated diterpenes such as grayanotoxins.

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Fumaric, palmitic, oleic and abscisic acids and methyl and ethyl hydrogen succinates were isolated from seedlings of dwarf pea (Pisrun sativunr L., var. Progress No. 9), grown under red light, as growth inhibitors which interfered with the responses of these plants to GA₃. Of the six compounds, fumaric acid did not show any inhibitory effect on stem elongation in the absence of GA₃.

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From seedlings of dwarf pea (Pisum satirvwn L., var. Progress No. 9) grown under red light, three neutral growth inhibitors were isolated which interfered with the responses of these plants to GA₃. The compounds were identified as β-sitosterol, α-stearoyl glycerol and pisatin, of which the glyceride produced remarkable inhibition when applied to terminal buds. Though its anti-gibberellin activity was not very strong, pisatin produced inhibition of the straightgrowth of Avena coleoptile segments caused by IAA.

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Methyl dl-l2-homo-l0-traps-juvenate (III) was synthesized from farnesol (IV) in eight steps involving stereoselective conversion of the traps-terminal methyl group to an ethyl group. The product (III) was less active than dl-C₁₇-Cecropia juvenile hormone on both Tenebrio molitor and Galleria mellonella.

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