Two carbohydrate rich fractions A and B were isolated from wheat gluten. Fraction B contained more lipid than fraction A. Lipid portion of fraction B consisted mainly of glycolipid and was fractionated into five fractions by thin-layer chromatography. The two main fractions were extracted and determined to be galactolipid and glucolipid, respectively, by the analyses of fatty acid and sugar components by gas chromatography. Defatted fraction A was assumed to consist of glycoprotein. After complete pronase digestion of defatted fraction A, the remaining glycopeptide moiety was isolated by column chromatography on DEAE-cellulose followed by gel filtration through Sephadex G-25. The amino acid and sugar components of the glycopeptide were investigated.

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In the present work the reaction of myosin with β-naphthoquinone-4-sulfonic acid (NQS) and the effect of modification of myosin with NQS on some physico-chemical properties of myosin were studied. The effects of several bivalent metal ions on ATPase activity of NQS-modified myosin were also investigated.
1) The reactivity of myosin by addition of NQS was at the maximum at pH 9.7.
2) The amount of NQS bound to myosin was greater at lower ionic strengths than at higher ionic strengths.
3) The reduced-viscosity of myosin increased with the increase in the number of amino groups modified with NQS.
4) The solubility of myosin at lower ionic strength (0.2M KCl) decreased with the increase in the amount of amino groups modified with NQS.
5) The helical content of myosin did not undergo any appreciable change by the NQS-modification of amino groups.
6) The Ca²⁺-activated ATPase activity of myosin did not undergo any appreciable change by the NQS-modification such that approximately 10 moles of amino group per mole of myosin or less, whereas EDTA-activated ATPase activity was markedly inhibited. However, when more than 10 moles of amino group were modified with NQS, even Ca²⁺-activated ATPase activity was remarkably inhibited.
7) Under the presence of Cu²⁺, both Ca^2--activated and EDTA-activated ATPase activities were significantly inhibited by the modification of myosin with NQS.
8) Superprecipitation activity and ATP sensitivity of actomyosin were not substantially influenced by the NQS-modification of myosin.

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The systematic identification and determination of many kinds of pesticides were attempted by a combination of column, thin-layer and gas chromatography. Twenty-one pesticides in the second division^2)- e. g., α-, β-, γ-, _??_-BHC, trifluralin, CPA, nitrofen, endrin, dieldrin, dicofol, etc. were separated from 15 pesticides in the third division-e. g., dichlone, EPN, anilazine, chlorpropyrate, chlorpropham, folpet, barban etc., and pesticides in the third division were also separated from those in the fourth division-e. g., trietazine, prometryne, propazine, atrazine, BPMC, carbaryl etc. by column chromatography. Furthermore, these pesticides in the second and third divisions were separated from each other and determined by gas chromatography with ECD, FTD and FID, after division into 4 groups by TLC. Most of these pesticides were more than 90% recovered through the whole procedure.

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Arthrobacter paraffineus KY 4303, when grown on fructose as the sole carbon source, produced two novel glycolipids, both of which were different from trehalose-lipid produced from n-alkane and sucrose-lipids from sucrose by the same microorganism. Two kinds of glycolipids were isolated by repeating chromatography on silicic acid columns. One of the glycolipids (abbreviated as FL-1, having low polarity) was identified as fructose-6-corynomycolate and another (FL-2, having high polarity) was identified as fructose-1, 6-dicorynomycolate. Formation of fructose-lipids was also demonstrated in fructose grown cells of several strains of Corynebacteria, Nocardia, Mycobacteria and Brevibacteria.

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Synthesis of methyl vitamin A from β-irone is described.

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Microorganisms which require oleic acid for the formation of antibiotics were screened. Streptomyces sp. No. 362, one of the selected organisms, produced antimicrobial substances only when oleic acid, palmitic acid or the high concentration of L-glutamic acid (or L-glutamine) was supplemented to the medium. The cellular fatty acid composition was changed by the supplement of these fatty acids, but not by L-glutamic acid (or L-glutamine). Antibioticproducing cells had about 4 to 10 times larger amino acid pools, especially L-glutamic acid pool, and hexosamine pools. The ability for L-glutamate uptake of cells grown in the oleic or palmitic acid supplemented medium was markedly enhanced and the efflux of the accumulated L-glutamate was reduced. The antibiotic produced by this strain was identified as one of the streptothricin-group antibiotics and the role of these additives in the antibiotic formation is discussed.

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Ascochlorin and its analogs were isolated from the filter cake of the fermented broth of a fungus, Ascochyta viciae Libert; the compounds obtained were ascochlorin, LL-Z1272δ, LL-Z1272 ε, ascofuranone, ascofuranol and a new analog, C₂₃H₃₁ClO₅. Some of these prenyl phenols show hypolipidemic activity in both normolipidemic and hyperlipidemic rats. Details of the structure determination for ascochlorin are presented. The structure of the new analog was elucidated as 4'-hydroxy-5'-hydroascochlorin.

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Two O-glucosides (I and II) have been isolated from buckwheat seeds by column chromatography on ion-exchange resins and cellulose powder. Hydrolysis with hydrochloric acid and β-glucosidase, and spectroscopic characterization revealed their structures to be o- and p-(β-glucopyranosyloxy) benzylamine. A salicylidene derivative of II was also prepared and characterized by spectral data. This is the first report of the occurrence of these two compounds in nature.

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The mass spectra of pestalotin and some related 4-methoxy-5, 6-dihydro-α-pyrones, each containing a substituent at the C-6 position, have been studied. The prominent peak was observed commonly at m/e 127 and was proved characteristic of the pyrone ring.

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Pentane inhibited the cell lysis of Micrococcus lysodeikticus by egg-white lysozyme, when added to the lysozyme solution before mixing the cells. The pentane inhibition was not observed when pentane was added either before to the cell suspensions or to the celllysozyme mixture. The degree of pentane inhibition was proportional to the concentration of pentane, and the maximum inhibition was achieved with about 5% pentane close to the saturation point. On the other hand, pentane did not inhibit the hydrolysis of glycol chitin by the lysozyme, showing that the β-1, 4-glucosaminidase activity of lysozyme remained unchanged. The inhibitory action of pentane on the lysozyme-induced cell lysis was of a competitive nature. The pentane inhibition had no pH-dependence, but it was influenced by the ionic strength of the buffer used as solvent.
When the lysozyme solution was treated with pentane, a characteristic ultraviolet spectrum of lysozyme was produced; a blue shift with a minimum at 280nm and a trough at 291nm. The degree of spectral change at 280nm depended on the concentration of pentane. Pentane was, therefore, found to interact with egg-white lysozyme to affect the conformation and enzymatic activity of lysozyme. The mechanism of pentane inhibition on the lysozymeinduced cell lysis was discussed.

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The lipid compositions, fatty acid compositions, positional distributions of fatty acids in glycerides, and molecular species of phospholipids of L. starkeyi, cultured in the glucose sufficient and the glucose deficient media were compared.
Under the glucose sufficient condition, the triglyceride content increased, accompanied by the remarkable increase of C_16:0-C_18:1-C_18:0. The phospholipid content also increased with the variations of the compositions of molecular species in phosphatidylethanolamine and phosphatidylcholine.
Under the glucose deficient condition, the triglyceride content remarkably decreased, especially in C_18:1-C_18:1-C_18:1. The compositions of phospholipid molecular species were considerably different from those of the glucose sufficient condition.

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An endo β-1, 6-glucanase (β-1, 6-glucan glucanohydrolase, E. C. 3. 2. 1.) has been purified from the culture filtrate of a strain resembling Rhizopus chinensis in homogeneous form. The procedures involved ammonium sulfate fractionation followed by column chromatography of DEAE-cellulose, CM-Sephadex C-50 and BioGel P-60.
Various physicochemical and chemical characteristics of the enzyme have been made clear, including complete amino acid composition. Optimum pH, optimum temperature, apparent activation energy for activity, Km and V_max are 5.5_??_6.0, 60°C, 4.39 Cal per mole, 9.39×10^-3_M glucose equivalents (0.169%) and 43.13 International Units, respectively. The enzyme required no metal ions for its activity, and it hydrolyzed β-1, 6-glucan larger than gentiotetraose, forming gentiobiose and gentiotriose as main products.

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Isosclerone, mp 74_??_76°C, [α]¹⁵_D+19°, a new metabolite of Sclerotinia sclerotiorum, was isolated and its absolute structure was determined as (4 S)-3, 4-dihydro-4, 8-dihydroxy -l(2H)-naphthalenone. It stimulated the root elongation of rice seedlings by ca. 30% at concentrations of 1_??_10ppm, and inhibited the growth of shoots and roots at high concentrations above 50ppm.

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A new compound was isolated from leaves of peanut. Its structure was determined as o-(malonylamino) benzoic acid on the basis of physicochemical evidences.

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The synthesis and biological activities of 2, 2-dimethyl-3, 3-dichlorocyclopropane carboxylic esters are descrived.

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Molecular conformational transition of GDPMan and solution conformation of α-D-mannopyranose moiety in Man-1-P and GDPMan were examined in relation to other sugar nucleotides and phosphates. GDPMan and other sugar nucleotides examined revealed changes in the optical rotation in sigmoidal curve in water by addition of urea. The change was reversible without significant decomposition and is attributable to dissociation of an ordered form into a random form. Optical conformational values [K]²¹_D in 8M urea solution were +116° for GDPMan, +58°_??_+79° for UDPGlc, +79° for UDPGal, +135°_??_+143° for UDPGlcNAc, and +138°_??_+155° for UDPGIcA.
NMR analysis and periodate oxidation study revealed the ⁴C₁ conformation of α-D-hexopyranose moieties in Man-1-P, Glc-1-P, GDPMan, UDPGlcNAc and UDPGalNAc.

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The electronic and hydrophobic substituent parameters of a number of o-, m- and p-substituted phenyl N-methylcarbamates were estimated by measuring the alkaline catalyzed hydrolysis rate constant and 1-octanol/water partition coefficient. Since some o-substituted derivatives are very potent insecticides, emphasis was placed on determining the ortho substituent effects in terms of the existing free-energy related parameters. The information obtained should be useful in structure-activity studies of carbamate insecticides.

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Immobilization of D-amino acid oxidase was investigated by covalently binding the enzyme to cyanogen bromide activated polysaccharides. Among polysaccharides tested, Sepharose 6B was found to be the best carrier.
Some enzymatic properties of the immobilized enzyme were investigated and compared with those of the native enzyme. The optimum pH of the immobilized enzyme was shifted by 0.5pH units to the acid side in comparison with that of the native enzyme. With regard to substrate specificity, heat stability and effect of temperature, no significant differences were observed between the immobilized and native enzymes.
The immobilized enzyme was conveniently used for a determination of D-amino acids and an analysis of optical purity of L-amino acids.

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