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Biomedical subjects

S Inouye

Publications and source records attributed to S Inouye.

At least 469 records · Page 26Linked to original sources

An ultrastructural study on the ear cartilage of rabbits after the administration of papain. Appearance of cross-striated collagen segments of an atypical FLS-type.

Crude papain was administered intravenously to young rabbits and the cartilage of the collapsed ear was examined electron-microscopically. Degeneration and recovery of chondrocytes, and decrease in and recovery of the electron-density of elastic fibers, were observed during the collapse and restoration of the ear. Some samples were stained with ruthenium red. In the collapsed ear, with a marked decrease of proteoglycan in the cartilage, loss of ruthenium red-positive granules was observed in the extracellular matrix. Collagen fibrils in the cartilage appeared to be somewhat increased in number, some of their diameters became slightly greater, and a part were assembled into bundles, occasionally accompanied by periodic cross-striation. Decrease of proteoglycan in the cartilage matrix probably brought about the unmasking and the assembly of collagen fibrils. In one of the experimental animals, collagen fibrous segments of an atypical fibrous long spacing (FLS-)type with symmetrical cross-striation were found around the chondrocytes in the ear cartilage, during the period of recovery. Some kind of the endogenous sulfated carbohydrate may have acted to affect the arrangement of type II collagen or procollagen molecules newly produced by the recovering chondrocytes.

Animals↗

Structure and function of the PHO82-pho4 locus controlling the synthesis of repressible acid phosphatase of Saccharomyces cerevisiae.

pho4 mutants of Saccharomyces cerevisiae, although rare among phosphatase-negative mutants isolated from wild-type strains, were isolated efficiently from pho80, pho85, or pho80 pho85 strains. The distribution of these pho4 mutants over the pho4 locus was determined by analyzing random spores of two- and three-factor crosses. The pho4-4 mutation confers temperature-sensitive synthesis of repressible acid phosphatase. An intragenic suppressor for the pho4-12 allele results in the temperature-sensitive synthesis of repressible acid phosphatase. Recombination between these sites occurs at 1.0 to 3.0%, the highest for any pair of sites within the pho4 locus. All these results strongly indicate that the information of the pho4 locus is translated into a protein. The PHO82 site was mapped inside the pho4 locus by random spore analysis. The order met10-pho4-1PHO82-1-pho4-9 on the right arm of chromosome VI was confirmed by tetrad analysis. Doubly heterozygous diploids, pho3 PHO82c PHO4+/pho3 pho82+ pho4, produce variable amounts of repressible acid phosphatase under repressive conditions depending on the combination of PHO82c and pho4 alleles. This phenomenon may reflect the constitutive production of the pho82+-pho4 product in the repressed condition, which interferes with the function of the PHO82c-PHO4+ product. The earlier model for the function of the PHO82-pho4 cluster, in which the PHO82 site acts as an operator of the pho4 gene, has been revised to a model in which the PHO82 site codes for the part of the pho4 protein that has affinity for the regulatory protein encoded by the pho80 and pho85 genes.

Acid Phosphatase↗

Molecular cloning of TOL genes xylB and xylE in Escherichia coli.

The xylB and xylE genes in the TOL plasmid of Pseudomonas putida mt-2, which code for benzyl alcohol dehydrogenase and catechol 2,3-oxygenase, respectively, were cloned onto plasmid pBR322 in Escherichia coli for detailed mapping. The xylB gene was mapped in a 2.9-kilobase region within the BamHI BC fragment of pTN2, an in vivo RP4-TOL recombinant, whereas the xylE gene was mapped in a 1.8-kilobase region within the BamHI BD fragment. The directions of transcription of these genes were deduced from the expression of the cloned genes which had been ligated in orientations opposite pBR322 at its BamHI site within the tetracycline resistance gene. The xylB and xylE genes are inducible by a specific inducer of the TOL pathway genes in the RP4-TOL recombinant, whereas they are not inducible in the pBR322-TOL hybrids. The regulatory regions involved in expression of the xylB and xylE genes do not appear to be located in the vicinity of the structural genes. Catechol 2,3-oxygenase formed in E. coli carrying an xylE-containing plasmid is similar, or identical, to that formed in P. putida carrying the TOL plasmid.

Alcohol Oxidoreductases↗

Molecular cloning of gene xylS of the TOL plasmid: evidence for positive regulation of the xylDEGF operon by xylS.

The xylDEGF operon and the regulatory gene xylS of the TOL plasmid found in Pseudomonas putida mt-2 were cloned onto Escherichia coli vector plasmids. A 9.5-kilobase fragment, derived from the TOL segment of pTN2 deoxyribonucleic acid, carried the xyl genes D, E, G, and F, which encode toluate oxygenase, catechol 2,3-oxygenase, 2-hydroxymuconic semialdehyde dehydrogenase, and 2-hydroxymuconic semialdehyde hydrolase, respectively. The enzymes were noninducible unless a 3-kilobase PstI fragment, derived also from the TOL segment, was provided in either cis or trans. The PstI fragment appeared to contain the regulatory gene xylS, which produced a positive regulator. The regulator was activated by m-toluate or benzoate, but not by m-xylene or m-methylbenzyl alcohol. the map positions of xylG and xylF were also determined.

Carboxylic Acids↗

Development-specific protein S of Myxococcus xanthus: purification and characterization.

Protein S, a development-specific protein of Myxococcus xanthus, was purified from the cells of a late stage of development and crystallized. Its circular dichroism spectra indicated that protein S had a high content of beta-structure in both the presence and absence of calcium ion, which is required for self-assembly of protein S on the myxospore surface. Its amino and carboxyl terminal sequences were determined to be alanine-aspartic acid-isoleucine-glycine-valine-alanine-methionine-asparagine-asparagine-aspartic acid-threonine-serine-serine and isoleucine-arginine (isoleucine, serine), respectively. When protein S (molecular weight, 23,000) was digested with trypsin, a trypsin-resistant core of 10,000 molecular weight was obtained. The core peptide was purified, and its amino acid composition was compared with that of protein S. The core peptide was capable of self-assembly on the spore surface in the presence of calcium ion and competed with protein S for binding on the spore surface. The ratio of affinity to the spore surface for protein S to that for the core peptide was 1.55.

Amino Acid Sequence↗

Simple technique for separation of concentrated immunoglobulin M fractions by multi-sample gel chromatography and its application to rubella serodiagnosis.

A simple technique has been developed with which five serum specimens can be chromatographed at one time and concentrated immunoglobulin M fractions can be obtained without using fraction collectors and ultraviolet monitors. When applied to the detection of rubella immunoglobulin M antibody, this technique gave results comparable to the sucrose gradient centrifugation method.

Antibodies, Viral↗

Difference in antibody reactivity between complement fixation and immune adherence hemagglutination tests with virus antigens.

Complement-fixing (CF) immunoglobulin M antibody to infantile gastroenteritis virus (a rotavirus) did not show the reactivity of immune adherence hemagglutination (IAHA). Early immunoglobulin G CF antibody produced both in patients and in guinea pigs experimentally infected with Japanese encephalitis virus (a flavivirus) had weak reactivity in IAHA test. However, late antibody showed higher titers by IAHA than by CF. These results suggested that early antibodies with lower affinity are inefficient in the IAHA reaction. The implications of this study are: (i) a low ratio of IAHA/CF antibody titers in a serum suggests a recent rotavirus infection; (ii) the IAHA reaction is more type specific than the CF reaction for identifying the serotype of antigenically cross-reacting viruses with hyperimmune sera.

Animals↗

Studies on a new aminoglycoside antibiotic, dactimicin. II. Isolation, structure and chemical degradation.

A new aminoglycoside antibiotic, dactimicin produced by a Dactylosporangium matsuzakiense SF-2052 has been isolated by column chromatography on a cation-exchange resin and CM-sephadex. The structure of dactimicin was determined to be 4-amino-1,4-dideoxy-3-O-(2,6-diamino-2,3,4,6,7-pentadeoxy-beta-L-lyxo- heptopyranosyl)-1-[(N-formimidoylglycyl)-methylamino]-6-O-methyl-L-chiro-inosit ol. Alkaline hydrolysis of dactimicin afforded 1-N-(N-formylglycyl)fortimicin B, fortimicin B, fortimicin A and an acyl migration product, 2'-N-(N-formylglycyl)fortimicin B.

Aminoglycosides↗

Studies on SF=1902 A2 A5, minor components of SF-1902 (globomycin).

Four members of globomycin, SF-1902 A2, A3, A4a and A4b were newly isolated from the culture of Streptomyces hygroscopicus SF-1902. These minor components shared four amino acids in common and the fifth was either valine or allo-isoleucine. The fatty acid moiety varied from 3-hydroxy-2-methylheptanoic acid in A2 to 3-hydroxy-2-methylundecanoic acids in A4b. The length of alkyl chain greatly affected the antibacterial activity, and maximum activity was shown by the homologue (A5) possessing the longest alkyl chain.

Acetylation↗