The effects of oral administration of hot water extract from autologous lysate of Lactobadllus casei (LEx) on the systolic blood pressure (SBP) were studied in spontaneously hypertensive rats (SHR). Oral doses of 10 mg/kg of LEx produced a significant decrease of the SBP of SHR, but LEx had no effect in normotensive rats. The long-term administration of LEx (1 or 10 mg/kg/day) to SHR from 5 to 17 weeks after birth suppressed the development of hypertension. LEx dialysed against distilled water was separated into a polysaccharide fraction (SG-1), a protein fraction (PR-1), and a nucleic acid fraction (NA-1), and SBP-lowering effects of these materials were investigated in SHR at the same dose (10 mg/kg). The most effective material of these three was SG-1.

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In order to elucidate the structure-activity relationship of griseofulvin (1), (±)-6'-demethyl analog (3), 2'-demethoxy-6'-demethyldihydro analog (4), (±)-dechloro-6'-ethyl analog (5), (±)-dechloro-6'epi-ethyl analog (6), (±)-6'-ethyl analog (7) and (±)-6'-epi-ethyl analog (8) were synthesized by a Diels-Alder cycloaddition of alkylidene ketones (16, 17, 18, 19 and 20) with modified 1, 3-butadienes (21 or 22). Their biological activities were examined against fungi.

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Differential scanning calorimetry (DSC) thermograms of soybean protein isolate developed two peaks corresponded to 115 and 75 globulin, the denaturation temperatures of which were 93.3 and 76.5°C, respectively, with 94% water. These peaks shifted to higher temperatures with lower water contents of the sample. At 47% water, there were two peaks, at 149 and 118.7°C, and at 11% water, there was one peak at 180°C. The DSC thermogram measured during cooling and reheating gave no peak. The soybean protein isolate was heated with 24.5% water at 100°C and then mixed with more water to the water contents of 94%. This sample gave two peaks at temperatures close to those of the original soybean protein, indicating that the soybean protein was not denatured at temperatures even above 100°C when the water content was low.

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To learn of possible contributions of amide side-groups of asparagine and glutamine residues to viscoelastic properties of food proteins, lime-processed gelatin, which has lost these amide side-groups, was amidated by reaction with ammonia and the water soluble carbodiimide, 1-ethyl-3-dimethylaminopropyl carbodiimide (EDC). Depending on the quantity of EDC used, 13 to 40.3% of carboxyl side-groups of gelatin was amidated without intra- and inter-molecular cross-linkages, as judged from analyses of free-amino groups, gel-filtration chromatography, and sodium dodecyl sulfate-polyacrylamide gel-electrophoresis. The amidated gelatins had higher isoionic points as expected, but their regeneration of the triple helical structure of collagen was prevented as judged from analyses of circular dichroism. Gels made from amidated gelatins showed fairly high viscosity but low gel strength.

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The sweet protein monellin consists of two noncovalently associated polypeptide chains, the A chain of 44 amino acid residues and the B chain of 50 residues. Two different primary structures have been reported for each of these chains. The complete amino acid sequence of monellin was determined by a combination of FAB- and ESI-mass spectrometry, and by automatic Edman degradation.

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A cDNA of insulin-like growth factor (IGF)-I mRNA was obtained from a rat liver cDNA library. This cDNA contained a 5' terminal sequence of 48 base pairs complementary to a sequence in the 3' terminal region (an inverted repeat sequence) except for one nucleotide insertion in the 3' region. Base sequence analysis of this cDNA, northern blot analysis of rat liver mRNA using a probe specific to 5' region of cDNA, base sequence studies of the 5' upstream region of a clone of the rat IGF-I gene, and some other studies suggested strongly that the inverted repeat sequence of the IGF-I cDNA used was introduced artificially during preparation of the cDNA library.

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The structures of three novel phytotoxins named (-)-mycousnine (II), (+)-isomycousnine (III) and (+)-oxymycousnine (IV), from the phytopathogenic fungus Mycosphaerella nawae, were elucidated on the hasis of spectroscopic and chemical evidence. ¹H- and¹³C-NMR signals of II, III and IV were assigned by ¹H-¹³C COSY, ¹³C-{¹H} LSPD, HMBC and NOESY. II and III were obtained directly from (+)-usnic acid (I) by heating with 15% hydrogen chloride in dry MeOH, and IV from II by H₂O₂ oxidation in pyridine. Methanolysis of IV gave a novel enonediol (V). II and III showed potent antimicrobial properties. These new metabolites are the first usnic acid derivatives isolated from fungi.

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The Zygosaccharomyces rouxii plasmid pSB3 is one of the yeast plasmids resembling 2-μm DNA. The presence of a cw-acting locus needed for stable maintenance of pSB3 has been expected by analogy with the functions encoded by other yeast plasmids such as 2-μm DNA and pSRl. We found such a locus and designated it STB-SB3. The STB-SB3 locus was delimited within 371 bp in a unique region of pSB3. This region is included in the plasmid region where no transcript was detected. No prominent feature of the nucleotide sequence was found in this region except for a direct repeat with 65% homology consisting of 27 bp and 29 bp. This is in clear contrast with the structure of the STB locus of 2-μ DNA which has five and a half tandem repeats consisting of a highly homologous 62 bp sequence. By analyzing the sites hypersensitive to nucleases using partially purified nuclei containing pSB3, the STB-SB3 locus was found not to be tightly folded into a nucleosome structure.

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Several microorganisms that produced levan-degrading enzyme were isolated from soil and the enzymes could be classified into several types according to the products from levan. Among these enzymes a levanase from Streptomyces sp. No. 7-3 was purified to homogeneity, shown by disc-electrophoresis. The molecular weight of the enzyme was 54, 000 by SDS-polyacrylamide gel electrophoresis, and 57, 000 by gel filtration. The isoelectric point of the enzyme was pH 4.7. The enzyme was most active at pH 6.5 and at 40°C, and stable up to 40°C and from pH 5.5 to pH 8.5. The enzyme hydrolyzed levan to produce levanbiose predominantly. Fructose (F, 3%) and levantriose (F3, 17%) were also produced in addition to levanbiose (F2, 80%).

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During the fermentation of 2-keto-L-gulonic acid (2KGA) from L-[U-¹⁴C]sorbose by the 2KGA-producing mutant UV10, derived from G. melanogenus IFO 3293, 40% of the metabolized substrate was converted to ¹⁴CO₂. The CO₂ evolved was mainly via the pentose phosphate pathway and partly via the intermediates such as L-sorbosone or the by-products of 2KGA formation. CO₂ evolution from 2KGA was not observed.

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Defense against insect attack was investigated for the lipid oxidation products made by soybean seed lipoxygenases, to study the physiological role of the enzymes in seeds. The repellent effect against bean bugs (Riptortm clavatus Thunberg), a major soybean pest, was observed in products of linoleic acid oxidation by lipoxygenases such as linoleic acid monohydroperoxides and hexanal. Bean bugs preferred lipoxygenase isozyme (L-1, L-2, and L-3)-null seeds, especially L-2 null seeds, more than normal soybean seeds, although no significant difference was observed in feeding preference at the repening period. The lipid peroxidation products of lipoxygenases, such as linoleic acid hydroperoxide and hexanal, also repelled two species of leaf beetles that do not usually feed on soybean seeds, and the threshold value for the oligophagous strawberry leaf beetles (Galerucella vittaticollis Baly) was lower than that for the polyphagous false melon beetles (Atrachy a menetriesi Falderman). These results suggested that the lipid oxidation products repelled the tested insects and that the soybean seed lipoxygenases could act defensively, although the effects of the products on the soybean pest insects was not great.

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Twelve γ-, δ- and ε-monoterpenelactones were synthesized, with seven compounds (5, 6, 7, 8, 13, 13', and 15) being newly formed. The odor of the monoterpenelactones was found to be dependent on the size of their rings and their conformation. Substitution of the equatorial methyl group at C(3) in the δ- and ε-monoterpenelactones with a planar molecular shape was necessary for the monoterpenelactones to produce a pronounced maple-tike odor.

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Comparative studies were made of the polymerization of L-aspartic and L-glutamic acid dialkyl esters using polyethylene gl¥ col-modified papain as a catalyst in phosphate buffer (pH 7.5) and in benzene. Changes in the substrate specificity of papain and in the composition of oligomerized products were observed. In the buffer, the diethyl and di-n-propyl esters of L-glutamic acid were sufficiently converted to high molecular weight oligomers with the accumulation of dimer and trimer, but L-aspartic acid esters were very poor substrates. In benzene, L-aspartic acid esters became more reactive than L-glutamic acid esters. In particular, from L-aspartic acid dimethyl ester the product, which was mainly composed of heptamer to decamer, was obtained in a 90% yield. The reaction in benzene required desalted substrates and a small amount of water to proceed extensively.

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The theanine (THE: γ-glutamylethylamide) accumulation level was greatly increased in tea callus when ethylamine hydrochloride (EtNH₂•HCl) was added to the medium. The optimum temperature for THE accumulation was the same temperature (25°C) as for growth of callus. Little THE was discharged into the medium. Dark culture was better than illumination for the accumulation of THE (201 mg/g dry wt.). These results suggested that THE synthetase had a positive activity, the decrease of THE content in callus was caused by the lowering of EtNH₂ biosynthesis level, and temperature and illumination strongly affected THE accumulation.

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Colloidal calcium phosphate (CCP)-increased casein micelle dispersion (CMD) was prepared by adding calcium chloride and dipotassium phosphate to CMD adjusting the pH to 6.7. The content of casein aggregates cross-linked by CCP in casein micelles was increased from 49.3 to 68.3% by adding calcium and phosphate to CMD. The amount of serum casein released from casein micelles on cooling decreased with increasing CCP content. Since it is probable that β-casein is only released from β-casein which is not cross-linked by CCP in casein micelles, β-casein in casein micelles was divided into the three types: cross-linked by CCP; not cross-linked and released on cooling; not cross-linked and not released on cooling. When the CCP content was increased to a large extent, β-casein released on cooling decreased from 31.8 to 2.1% of the total β-casein, while β-casein cross-linked by CCP and β-casein which is not cross-linked and not released on cooling were increased from 46.2 to 69.9% and from 22.0 to 28.0% of the total β-casein, respectively.

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Under aerobic conditions, washed intact cells of Thiobacillus ferrooxidans AP19-3 solubilized copper enzymatically from a copper concentrate containing Cu(20.48%), Fe(31.61%), 8(38.22%), Pb(3.84%), and Zn(4.22%). The optimum pH of copper solubilization from copper concentrate was at pH 3.0. In contrast, under anaerobic conditions or under aerobic conditions in the presence of sodium cyanide, inhibitor of iron oxidase, the amount of copper solubilized enzymatically from the ore markedly decreased, indicating that iron oxidase is involved in the copper solubilization. Under the conditions under which iron oxidase of the cells cannot operate, Fe²⁺ and Cu⁺ ions were produced enzymatically, suggesting that a hydrogen sulfide: ferric ion oxidoreductase (SFORase) was involved in this copper solubilization from the ore. A short treatment of the strain with 0.5% phenol completely destroyed the SFORase. However, this treatment did not affect the iron oxidase of the cells. A concomitant loss of the activity of copper solubilization from the ore was observed in 0.5% phenol-treated cells. The results strongly suggest that both iron oxidase and SFORase are crucial in copper ore leaching by T. ferrooxidans AP19-3.

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The amino acids of Lady Amherst's pheasant and golden pheasant egg-white lysozymes have been sequenced. The carboxymethylated lysozymes were digested with trypsin followed by sequencing of the tryptic peptides. Lady Amherst's pheasant lysozyme proved to consist of 129 amino acid residues, and a relative molecular mass of 14 423 Da was calculated. This lysozyme had 6 amino acids substitutions when compared with hen egg-white lysozyme: Phe3 to Tyr, HislS to Leu, Gln41 to His, Asn77 to His, Gin 121 to Asn, and a newly found substitution of Ile124 to Thr. The amino acid sequence of golden pheasant lysozyme was identical to that of Lady Amherst's phesant lysozyme. The phylogenetic tree constructured by the comparison of amino acid sequences of phasianoid birds lysozymes revealed a minimum genetic distance between these pheasants and the turkey-peafowl group.

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Microorganisms that produce ascorbic acid-2-phosphate (AsA2P) from ascorbic acid (AsA) and ATP were screened from our culture collection. Of 715 strains, three microorganisms, Pseudomonas azotocolligans KY4661, P.paucimobilis KY4084, and an unidentified bacterium KY3132 were selected as AsA2P-producers. When using 50 mg (wet weight) of P. azotocolligans cells per ml as the enzyme source, 3.7 mM AsA2P were produced for 23 hr, from 30 mM AsA and 40 mM ATP. From analytical data of the purified product from the reaction mixture, these microorganisms phosphorylated AsA at the C-2 position specifically.

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An isoamylase-hyperproducing mutant, strain MI-414, was isolated by treating Pseudomonas amyloderamosa SB-15 with N-methyl-N'-nitro-N-nitrosoguanidine. Strain MI-414 produced 10-fold more isoamylase than strain SB-15. SI nuclease mapping of isoamylase mRNAs from the strains showed that the level of isoamylase mRNA was higher in MI-414 than in SB-15. The copy number of the isoamylase gene (iam) was not changed by the mutation. Moreover, the nucleotide sequence of the promoter region of iam, the transcription initiation site, and the expression patterns of iam in the presence of glucose and of maltose were the same in these strains. However, the half-lives of iam-mRNAs in SB-15 and MI-414 were approximately 3 and 22min, respectively. Therefore, hyperproduction of isoamylase in the mutant results, at least partly, from the greater stability of its mRNA.

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To investigate the immunochemical properties of proteins reacted with malondialdehyde (MDA), which is a major degradation product of lipid oxidation, the antibody responses of mice immunized with MDA-modified bovine serum albumin (BSA) were examined. The specific IgE response to MDA-BSA was 4 to 8 times higher than that to native BSA, suggesting that the specific IgE antibody response to MDA-modified protein was enhanced by MDA bound to the surface of the protein. The antibodies to MDA-BSA did not distinguish the modified protein from the native one, and the antibodies raised against the modified proteins were not specific for the MDA portion but were for the carrier proteins.

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Autopolyploid strains were isolated from auxotrophic mutants, no. 77 (lys^-), no. 77-25(lys^- met^-), and a cycloheximide 500μg/ml resistant mutant, CR50 derived from T. reesei QM 9414 by 0.1% (w/v) colchicine treatment for 24 hr and 72 hr at 30°C. An autopolyploid strain, 77-25(24)-!, showed higher cellulase productivity especially in Avicel-hydrolyzing activity. When autopolyploid strains were treated with benomyl, trypan blue, and coumarin, various genetic variants in growth rate, conidial formation, and cellulase productivity could be isolated in addition to the 3 types of fruit-body-like structures. It was considered that autopolyploid formation by colchicine and benomyl treatment of autopolyploid strains were effective in breeding of T. reesei QM 9414.

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The administration of 5-hydroxy-L-tryptophan to growing cells yielded a new blue pigment. The chemical structure was determined to be 5-(5-hydroxyindol-3-yl)-3-(5-hydroxy-3-oxoindolylidene)-4-pyrroline-2-one, mainly by using proton- and carbon 13-NMR. Feeding experiments of 5-hydroxytryptophan labeled with deuterium and carbon-13 unambiguously demonstrated that the hydroxylation of tryptophan was the first step for violacein biosynthesis. No incorporation of 5-hydroxy-[4, 6-²H₂]tryptamine suggests that decarboxylation of 5-hydroxy-L-tryptophan was not the second reaction, but should take place at a later stage in the pathway of violacein formation. 5-Hydroxy-[4, 6-²H₂]indole was not incorporated, indicating that an enzyme like tryptophanase was unlikely to have been involved in violacein biosynthesis.

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Adults of the geometrid moth, Arichanna gaschkevitchii, were found to store grayanoid diterpenes originating from the larval host plant, Pieris japonica (Ericaceae), in the body tissue. The compounds were characterized as asebotoxins I and IV, grayanotoxin III, rhodojaponin III, kalmitoxin I and two new analogs, arichannatoxin I and II. The content of the total grayanoid analogs in the body tissue was as high as 300 μg/moth. The most predominant component, asebotoxin I (200 μg/moth), strongly deterred feeding of house lizards, which suggests a defensive role against predatory animals.

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Many strains of the genus Ustilago were found to be good producers of organic acids, that is, itaconic, l-tatartaric, l-2-hydroxyparaconic, and L-malic acids. Itatartaric and 2-hydroxyparaconic acids were invariably produced together with itaconic acid. From these findings and the results of the experiments with permeabilized cells of Ustilago cynodontis, the following metabolic sequence was assumed: i taconate→2-hydr ox y par aconate→itatartar ate, as a by-path from the tricarboxylic acid cycle.

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Ustilago cynodontis K320 was selected as the best strain for the production of l-itatartaric acid and its lactone, l-2-hydroxyparaconic acid, in shake culture under acidic conditions. Factors affecting the acid production were examined to optimize the culture conditions for maximal production of itatartaric and 2-hydroxyparaconic acids and efforts were made to simplify the recovery of the acids. Fermentation in a jar was continued until the accumulated itaconic acid and erythritol were completely consumed. 2-Hydroxyparaconic acid (49 g) was easily recovered as a crystalline mass (about 96% in purity) from 11 of the culture filtrate by a process consisting of concentration, lactonization of itatartaric acid to 2-hydroxyparaconic acid, and ethyl acetate extraction. Sodium itatartarate was prepared from the recovered 2-hydroxyparaconic acid by saponification.

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In the course of our screening program for inhibitors of soybean lipoxygenase, we isolated two new phenolic sesquiterpene ketones named turmeronol A and turmeronol B from the spice turmeric (dried rhizome of Curucuma longa L.). Their structures were determined to be 2-methyl-6-(3-hydroxy4-methyIphenyl)-2-hepten-4-one and 2-methyl-6-(2-hydroxy-4-methylphenyl)-2-hepten-4-one, respectively. Turmeronol A and turmeronol B inhibited soybean lipoxygenase at the IC₅₀ values of 16μM and 9 μM, respectively. These compounds prevented the autoxidation of h'noleic acid at a concentration of ca. 200 ppm.

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The influence of steric factors on the activity of chiral isomers on the N²-α-methylbenyl and -or N⁴-sec-butyl group of the 2, 4-diamino-6-chloro-s-triazines as the inhibitor of the Hill reaction was examined. The (S)-isomers for either chiral center were more active than the corresponding (R) -isomers. The N²-(S)-α-methylbenzyl-s-triazine compound, in spite of a change of the substituent of the N⁴-amino group, exhibited considerably high potency; in particular the N⁴-ethyl derivative (19) was the most potent inhibitor toward PSII. The level of optical discrimination of the receptor site for the chiral isomer of the a-methylbenzyl-s-triazines was greater than those for the sec-butyl derivatives, and their rates varied with the change of steric hindrance of the substituent at the other amino group. The structure-activity relationship for the s-triazine compounds tested involved the binding direction of the s-triazine inhibitor being determined by the difference in size of the substituent at each amino group. The amino group with a small substituent offerring low steric hindrance is placed in a narrow binding region (N-region) of the receptor site in PSII protein, and the other amino group is placed in a wide region (W-region), the optical discrimination to each region depending on the steric suitability of the other one.

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The geometrical isomers of O-4-tert-butylcyclohexyl methylthiocarbamate were prepared by way of the corresponding dithiocarbonates. The O-trans-isomer was obtained from a mixture of cis- and trans-4-tert-butylcyclohexanols via an alkoxide formation involving biassed equilibration, whereas the O-cis isomer was from the cis-cyclohexanol via an alkoxide formation free from equilibration.
The acid-catalyzed rearrangement of the O-cis thiocarbamate gave a 1:3 mixture of S-cis- and S-trans-4-tert-butylcyclohexyl methylthiocarbamates, whereas that of the O-trans thiocarbamate afforded a 9:1 mixture of S-cis and S-trans products.
These results, together with the data from a study on the reactions of O-cis-3, 3, 5-trimethylcyclohexyl methylthiocarbamate and the O-neopentyl analog, indicate that the acid-catalyzed rearrangement proceeded mostly through an S_N2 type of transalkylating mechanism to give the S-isomer in the case where the approach of nucleophiles was not sterically blocked, otherwise the reaction gave S_Nl-type products.

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Aminopeptidase T (AP-T) is a metallo-dependent dimeric enzyme of Thermus aquaticus YT-1, an extremely thermophilic bacterium. We cloned the AP-T gene from T. aquaticus YT-1 into Escherichia coli using a synthetic oligonucleotide as a hybridization probe. The nucleotide sequence of the AP-T gene was found to encode 408 amino acid residues with GTG as a start codon. The molecular weight was calculated to be 44, 820. The AP-T was overproduced in E. coli (about 5% of total soluble protein) when the start codon of the gene was changed from GTG to ATG, and the gene was downstream from the tac promoter. The AP-T expressed in E. coli was heat stable and easily purified by heat treatment (80°C, 30min). The N-terminal amino acid sequence of AP-T showed similarity with that of aminopeptidase II from Bacillus stearothermophilus.

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Interspecific protoplast-fusants between Aspergillus oryzae (yellow-spored, met^-) and Aspergillus sojae (white-spored, bio^-) were haploidized by benomyl. Throughout the haploidization trials, seventy-six white- or yellow-spored segregants were isolated from 9 stable green-spored fusants. All of the seventy-two color-segregants derived from 7 phenotypically A. oryzae-type fusants did show the A. sojae type alkaline proteinase. Gel-electrophoretic phenotypes of both alkaline and acid proteinases appeared to share a common behavior in fusion and haploidization, although pectin-lyase and the morphology of conidial walls behaved independently from each other in these processes. Productivities of some hydrolyzing enzymes in koji culture, especially peptidase, were found to be improved by interspecific fusion and subsequent haploidization. Productivities of kojic acid and aspergillic acid were found to be amendable through these process.

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A fungal metabolite, (6S, 1'S, 2'R)-6-(1', 2'-dihydroxypentyl)-4-methoxy-5, 6-dihydropyrane-2-one (LL-P88β, I), and its C₆-epimer (II) were synthesized by the chiron approach. The key intermediate, (2S, 3R)-2, 3-dihydroxyhexanal derivative (3), was prepared from D-glucose as a chiral building block and reacted with the dianion of ethyl acetoacetate to complete the formal syntheses of I and II.

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Ren-1 renin is synthesized in the kidney of every mouse. Ren-2 renin has been observed in the submandibular gland (SMG) of male mice carrying two renin genes. However, it is not known if Ren-2 renin is in the kidney and blood of the two-renin gene mice. In this study, a direct ELISA for Ren-2 renin (SMG renin) was established by a sandwich method. This ELISA could measure the Ren-2 active renin in the range from 1 to 100 ng and distinguish Ren-2 active renin from not only Ren-1 renin but also Ren-2 prorenin. By a combination of this assay system and conventional methods, the pro-form as well as the active form of Ren-2 renin was found in the kidney and plasma of male AKR mice carrying two-renin genes.

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Oxidation of short-chain iso-alkanes (isobutane, isopentane, 2-methylpentane, and 3-methylpentane) was studied with propane-grown resting mycelia of Scedosporium sp. A-4. Isobutane was oxidized to terf-butanol, but both isobutane and tert-butanol were not used for growth. Isopentane was oxidized to 3-methyl-l-butanol, 2-methyl-2-butanol, and 3-methyl-2-butanol but not to 2-methyl-l-butanol. 2-Methylpentane was oxidized to 4-methyl-l-pentanol, 2-methyl-2-pentanol, and 4-methyl-2-pentanol but not to 2-methyl-l-pentanol or 2-methyl-3-pentanol. 3-Methylpentane was not oxidized. Oxidation of branched alcohols was also studied.

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The mechanism for chrysodin antifungal action was studied by using Candida albicans. Chrysodin inhibited the incorporation of radioactive precursors into macromolecules in whole cells nonspecifically among various macromolecule species, i.e., DNA, RNA, protein, polysaccharide and lipid. It also inhibited cellular respiration with a more marked effect on exogenous than on endogenous respiration. On the other hand, chrysodin greatly enhanced the leakage of UV-absorbing materials from treated cells, although it had no effect on liposomal glucose leakage. Cells grown in the presence of low concentrations of chrysodin had significantly lower amounts of linolenic acid and linoleic acid than control cells. The addition of unsaturated fatty acids reversed to some extent the growth inhibition by chrysodin. These results suggest that the antifungal action of chrysodin is due to a change in the cell membrane permeability related to polyenoic fatty acid biosynthesis in the yeast cells.

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