• Journal of the Korean Chemical Society
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• v.34 no.6
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• pp.517-526
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• 1990

The crystal structures of two alditol acetates, D-glucitol hexaacetate and xylitol pentaacetate, have been determined by diffraction methods with Mo-K$\alpha$radiation, using direct methods for phase determinations. The crystal data are: for D-glucitol hexaacetate, P2$_1$, with a = 10.275 (2), b = 8.363 (1), c = 12.560 (5) $\AA;\beta$ = 95.97 $(2)^{\circ}$, Z = 2; for xylitol pentaacetate, P2$_1$/C with a = 18.126 (1), b = 11.422 (2), c = 8.649 (1) $\AA$, $\beta = 95.03 (1)^{\circ}$, Z = 4. Both molecules have extended zigzag carbon chain conformations which differ from previous studies of the structures of D-glucitol and xylitol and also differ from NMR studies on alditol acetates. The bond lengths and angles are normal, with mean values over both structures of C($sp^3)-C(sp^3): 1.514 (10),\; C(sp^3)-O: 1.444 (6),\; C(sp^2)-O: 1.347 (9),\; C(sp^2)=O: 1.197 (6),\; C(sp^2)-C(sp^3): 1.479(9){\AA},\; C(sp^3)-C(sp^3)-C(sp^3): 114.6 (17),\; O-C(sp^3)-C(sp^3): 109.4 (23),\; C(sp^2)-O-C(sp^3): 117.4 (6),\; O=C(sp^2)-O: 122.6 (6),\; C(sp^3)-C(sp^2)-O: 111.8 (7),\; C(sp^3)-C(sp^2)=O: 125.5 (4)^{\circ}$. The atoms of acetate groups are in coplanar. There are no particularly short intermolecular contacts and the molecules are held together by van der Waals force only.

• Korean Journal of Veterinary Research
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• v.17 no.1
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• pp.17-26
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• 1977

Parasites of wild animals are closely related with parasites of domestic animals. Wild animals take charge of an important role at parasitic infestation of domestic animals because of unrestrained movement. The authors carried out the work of actual condition of parasitic infestation on wild animals, total 1,014 cases, in the Korean Zoo. The results are summarized as follows: 1. Total rate of parasitic infestation was 36.1% with infestation of 366 among 1,014 cases. The rate of single infestation was 32.6% with infestation of 331 cases, double infestation 3.1% with 31 cases, triple infestation 0.2% with 2 cases and quadrople infestation 0.2% with 2 cases. 2. The parasites on the zoo animals were identified as follows: Lion: Sarcoptiform, Toxocara sp., Toxascaris leonina, Ancylostoma sp. and Isospora spp. Puma: Toxocara sp., Ancylostoma sp. and Isospora sp. Leopard: Toxocara spp., Ancylostoma sp., Trichuris sp., Dibothriocephalus sp. and Physaloptera sp. Wolf: Sarcoptiform and Dibothriocephalus spp. Fox: Trichuris sp., Capillaria aerophila, Spirocerca sp., Paragonimas kellicotti. Jackal: Sarcoptiform, Ascaris sp. and Echinococcus granulosus. Wild Cat: Dibothriocephalus sp. Tiger: Toxascaris leonina. Bear: Sarcoptiform, Metastrongylus apri, Ancylostoma sp. and Ascaris sp. Raccoon and Raccoon dog: Sarcoptiform, Paragonimus kelliotti, and Isospora sp. Boar: Oesophagostomum spp. and Eimeria spp. Mortkey: Sarcoptiform, Trichuris sp., Physaloptera spp.. Enterobius sp. and Isospora sp. Elephant: Sarcoptiform, Strongyloides sp. and Strongylus spp. Deer: Sarcoptiform, Strongyloides sp., Trichuris ovis, Mccistocirrus digitatus, Haemonchus sp., Oesophagostomum radiatum, Paramphistornum spp., Bunostomum phlebotomum, Fasciola hepatica and Eimeria spp. Bison: Sarcoptiform, Haernonchus sp., Marshallagia sp., Nematodirus sp. and Eimeria sp. Zebra: Strongylus sp. and Parascaris equorum. Goral and Barbary: Sarcoptiform, Haemonchus sp., Oesophagostomum venulosum, Moniezia sp. and Eimeria spp. Lama: Strongyloides sp. and Haemonchus sp. Kangaroo: Strongyloides sp. and Haemonchus sp. Camel: Strongyloides sp., Trichuris ovis and Eimeria sp. Peacock and the Other Birds: Sarcoptiform, Capillaria contorta, Capillaria caudinflata, Ascaridia spp., Heterakis spp., Hymenolepis sp., Eimeria spp., Histomonas, Ornithionyssus bacoti, Macrochelidae and Trichomonas. 3. Among the zoo animals, wild carnivora were infestated with the parasites which are common parasites of dogs and cats, wild herbivora were infestated with the parasites of herbivora domestic animals. and wild fowls were infestated with the parasites of domestic fowls.

• Korean Journal of Microbiology
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• v.45 no.4
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• pp.300-305
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• 2009

We constructed the deletion mutants of fission yeast Schizosaccharomyces pombe spNab2 gene that is homologous to poly(A)-binding protein NAB2 in budding yeast Saccharomyces cerevisiae, which plays crucial roles in mRNA 3' end formation and mRNA export from nucleus into the cytoplasm. A null mutant in an $h^+$/ $h^+$ diploid strain was constructed by replacing the spNab2-coding region with an $ura4^+$ gene using one-step gene disruption method. Tetrad analysis showed that the spNab2 is not essential for vegetative growth and mRNA export. However, over-expression of spNab2 cause the severe growth defects and intensive accumulation of poly(A) RNA in the nucleus. Also, the spNab2-GFP fusions were localized mainly in the nucleus. These results suggest that spNab2 is also involved in mRNA export out of the nucleus.

• International Journal of Industrial Entomology and Biomaterials
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• v.2 no.2
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• pp.161-166
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• 2001

The storage proteins of the mulberry longicorn beetle, Apriona germari Hope, were purified and characterized. Three kinds of storage protein (SP1, SP2 and Sp3) were purified from the last instar larval hemolymph of A. germari by the FPLC techniques, anion exchange chromatography and gel permeation chromatography. The SP1, SP2 and SP3 have a native molecular weight of 480, 440 and 420 kDa, respectively. In the SDS-polyacrylamide gel electrophoresis analysis, these storage proteins are composed of a single protein subunit with molecular weight of 90, 85 and 80 kDa, respectively. This result showed that the storage proteins are hexameric protein. The SP1 and SP2 were stained with Schiffs reagent, but SP3 was not stained. It can be assumed that SP1 and SP2 are glycoprotein. Western blot analyses using the each of polyclonal antiserum against purified SP1, SP2 and SP3 showed that the three antibodies reacted with the each of SP bands, respectively. Also, antibodies against SP1 and SP3 cross-reacted with the SP3 and SP1, respectively. However, SP2 was not cross-reacted with these two antibodies. Also, antiserum against SP2 did not cross-reacted with the SP1 and SP3.

• Microbiology and Biotechnology Letters
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• v.35 no.2
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• pp.104-111
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• 2007

In this study, aniline dioxygenase genes responsible for initial catabolism of aniline in Burkholderia sp. HY1 and Delftia sp. HY99 were cloned and the amino acid sequences were comparatively analyzed, which already have been reported as bacteria utilizing aniline as a sole source of carbon and nitrogen, B. sp. HY1 was found to have at least a plasmid, and the plasmld-cured strain, B. sp. HY1-PC obtained using mitomycin C was tested with wild type strain to investigate whether the former maintained the degradability for aniline. This proved that the aniline oxygenase gene from B. sp. HY1 was located in chromosomal DNA, not in plasmid DNA. Aniline dioxygenase small subunits from B. sp. HY1 and D. sp. HY99 were found, based on 146 amino acids, to share 79% similarity. Notably, ado2 genes from B. sp. HY1 and D. sp. HY99 which were found to be terminal dioxygenase of aniline dioxygenase small subunit showed 99% similarity in the deduced amino acid sequences with tdnA2 of Frateuria sp. ANA-18 and danA2 of D. sp. AN3, respectively. Besides, enzyme assay and amino acid sequence analysis of catechol dioxygenase supported the previous report that B. sp. HY1 might occupy ortho-cleavage pathway using catechol 1,2-dioxygenase, while D. sp. HY99 might occupy catechol 2,3-dioxygenase for meta-cleavage pathway.

• Journal of Environmental Health Sciences
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• v.11 no.1
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• pp.15-28
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• 1985

In order to analyze the water quality in artificial lakes in Chonnam area, a chemical and biological examination of Dongbock Lake and Changsung Lake was conducted from September to December 1983 and May 1984. A summary of the surveyed results is as follows 1. In Dongbock Lake, pH ranged from 7.2-8.1, D.O.: 8.2-12.6mg/l, B.O.D.: 4.4-22.1 mg/l, C.O.D.: 1.0-3.4rag/l, Cl$^-$: 5.9-11.9mg/l, Total-P: 0.001-0.071 mg/l, and Total -N: 0.016-0.697 mg/l, respectively. 2. In Changsung Lake, pH ranged from 7.2-8.1, D.O.: 8.1-9.8mg/l, B.O.D.: 0.9-2.9mg/l, C.O.D.: 1.9-3.4mg/l. Total- P: 0.006-0.016mg/l and Total -N:0.006-0.033mg/l, respectively. 3. The Phytoplankton identified in this investigation were distributed in a total of 46 genera and 76 spedes in Dongbock Lake 37 genera and 45 species in Changsung Lake. 4. In Dongbock Lake, it was found that the dominant algae were Melosira sp., Microcystis sp. and Synedra sp. in September Melosira sp. and Microcytis sp. in October, but Cymbella sp., Naviculla sp. and Nitzschis sp. were also observed in OctoberAsterionella sp., Melosira sp. and Microsystis sp. in November and Melosira sp., Asterionella sp sp. and Synedra sp. in December 1983. 5. In Changsung Lake, it was found that the dominant algae were Melosira sp., Lyngrbya sp. and Microcystis in September Melosira sp. and Synedra sp. in October and November and Melosira sp., Lyngbya sp. and Asterionella sp. in December 1983. The dominant algae were Melosira sp., Lyngbya sp. and Euglena sp. in May 1984. 6. It was found that the dominant algae in both Dongbock and Changsung Lakes were Microcystis sp., Melosira sp. and Asterionella sp.. Which are strongly related with water-bloom. Therefore, it could be suggested that the eutrophication phenomena is going to occur very easily in Dongbock Lake and possibly in Changsung Lake.

• The Korean Journal of Mycology
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• v.16 no.3
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• pp.157-161
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• 1988

The vegetative nuclear divisions in hyphae and chromosome numbers were studied with the aid of Giemsa-HCl techniques from 10 strains of Fusarium oxysporum. The entire nuclear division process occurred within an intact nuclear envelope like other fungus. The results confirmed that 2 strains(F. oxysporum S Hongchun D2, F. oxysporum S Jinyang 4) were n=4; 3 strains(F. oxysporum f. sp. lini KFCC 32585, F. oxysporum f. sp. melongenae KFCC 34743 and F. oxysporum f. sp. raphani) n=5; 2 strains(F. oxysporum f. sp. vasinfectum, and F. oxysporum f. sp. mori KFCC 34742) n=6; 3 strains(F. oxysporum f. sp. cucumerium, F. oxysporum f. sp.niveum, and F. oxysporum f. sp. pisi) n=7.

• Journal of Applied Biological Chemistry
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• v.61 no.1
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• pp.59-67
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• 2018

This study was conducted to isolate the cellulolytic bacteria able to grow on LB- Carboxymethyl cellulose (CMC) agar trypan blue medium from the mixed forest and Larix leptolepis stands. Three bacterial strains with high activity against both CMC and xylan were isolated. Both API kit test and 16S rRNA gene sequence analysis revealed that the three different isolates belong to the gene Bacillus. Therefore, the isolates named as Bacillus sp. EFL1, Bacillus sp. EFL2, and Bacillus sp. EFP3. The optimum growth temperature of Bacillus sp. EFL1, EFL2, and EFP3 were $37^{\circ}C$. The optimum temperature for CMCase and xylanase from Bacillus sp. EFL1 were $50^{\circ}C$. The optimum pH of Bacillus sp. EFL1 xylanase was pH 5.0 but the optimum pH of CMCase from Bacillus sp. EFL1 was pH 6.0. The optimum temperature of CMCase and xylanase from Bacillus sp. EFL2 was $60^{\circ}C$, respectively. The optimum pH of CMCase of Bacillus sp. EFL2 was 5.0, whereas xylanase showed high activity at pH 3.0-9.0. The optimum temperature for CMCase and xylanase of Bacillus sp. EFP3 was $50^{\circ}C$. The optimum pH for CMCase and xylanse was 5.0 and 4.0, respectively. CMCases from Bacillus sp. EFL1, EFL2, and EFP3 were thermally unstable. Although xylanase from Bacillus sp. EFL1 and EFP3 showed to be thermally unstable, xylanase from Bacillus sp. EFL2 showed to be thermally stable. Therefore, Bacillus sp. EFL2 has great potential for animal feed, biofuels, and food industry applications.

• Korean Journal of Microbiology
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• v.41 no.1
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• pp.13-17
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• 2005

The aim of this work was to investigate the N-terminal amino acid sequence of catechol 2,3-dioxygenase isolated from Delftia sp. JK-2, which could utilize aniline as sole carbon, nitrogen and energy source. Molecular weight of the enzyme was determined to approximately 35 kDa by SDS-PAGE. N-terminal amino acid sequence of C2,3O from strain JK-2 was $^1MGVMRIGHASLKVMDMDAAVRHYENV^{26}$, and exhibited high sequence similarity with that of C2,3O from Pseudomonas sp., Comamonas sp. JS765, Comamonas test-osteroni, or Burkholderia sp. RP007. Approximately 950-bp C2,3O was obtained through PCR using the primers derived from N-terminal amino acid sequence. Analysis of the DNA sequence revealed that the deduced 296 amino acid sequences were determined, and it showed $100\%$ identity with C2,3O from Pseudomonas sp. AW-2 and $97\%$ similarity with Comamonas sp. JS765.

• Journal of Microbiology
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• v.35 no.1
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• pp.53-60
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• 1997

Pseudomonas sp. P20 and Pseudomonas sp. DJ-12 isolated from the polluted environment are capable of degrading biphenyl and 4-chlorobiphenyl (4CB) to produce benzoic acid and 4-chlorobenzoic acid (4CBA) respectively, by pcbABCD-encoded enzymes. 4CBA can be further degraded by Pseudomonas sp. DJ-12, but not by Pseudomonas sp P20. However, the meta-cleavage activities of 2, 3-dihydroxybiphenyl (2, 3-DHBP) and 4-chloro-2, 3-DHBP dioxygenases (2, 3-DHBD) encoded by pcbC in Pseudomonas sp. P20 were stronger than Pseudomonas sp. DJ-12. In this study, the pcbC gene encoding 2, 3-DHBD was cloned from the genomic DNA of Pseudomonas sp. P20 by using pKT230. A hybrid plasmid pKK1 was constructed and E. coli KK1 transformant was selected by transforming the pKK1 hybrid plasmid carrying pcbC into E. coli XL1-Blue. By transferring the pKK1 plasmide of E. coli KK1 into Pseudomonas sp. DJ-12 by conjugation, a recombinant strain Pseudomonas sp. P20, Pseudomonas sp. DJ-12, and the recombinant cell assay methods. Pseudomonas sp. DJ12-C readily degraded 4CB and 2, 3-DHBP to produce 2-hydroxy-6-oxo-6-phenylhexa-2, 4-dienoic acid (HOPDA), and the resulting 4CBA and benzoic acid were continuously catabolized. Pseudomonas sp. DJ12-C degraded 1 mM 4CB completely after incubation for 20 h, but Pseudomonas sp. P20 and Pseudomonas sp. DJ-12 showed only 90% and Pseudomonas sp. DJ-12 had, but its degradation activity to 2, 3-DHBP, 3-methylcatechol, and catechol was improved.