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  • RH mapping  (5)
  • Poly(3-hydroxybutyrate)  (4)
  • Bacterioruberin  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Purification and properties of extracellular poly(3-hydroxybutyrate) depolymerases from Pseudomonas lemoignei
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 827 (1985), S. 63-72 
    Details
    ISSN: 0167-4838
    Keywords: (P. lemoignei) ; Extracellular enzyme ; Poly(3-hydroxybutyrate) ; d-(-)-3-Hydroxybutyrate oligomer hydrolase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4838(85)90101-3
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Degradation of poly(3-hydroxybutyrate) by poly(3-hydroxybutyrate) depolymerase from Alcaligenes faecalis T"1
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 880 (1986), S. 46-53 
    Details
    ISSN: 0304-4165
    Keywords: (A. faecalis) ; Extracellular enzyme ; Poly(3-hydroxybutyrate) ; Poly(3-hydroxybutyrate) depolymerase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0304-4165(86)90118-2
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  • 3
    Electronic Resource
    Electronic Resource
    Purification and characterization of extracellular poly(3-hydroxybutyrate) depolymerases (1995)
    Springer
    Journal of polymers and the environment 3 (1995), S. 13-21 
    Details
    ISSN: 1572-8900
    Keywords: Poly(3-hydroxybutyrate) ; poly(3-hydroxybutyrate) depolymerase ; extracellular enzyme ; N-terminal amino acid sequence ; enzyme purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Five extracellular PHB depolymerases of bacteria isolated from various sources were purified to electrophoretic homogeneity and compared with known extracellular PHB depolymerase fromAlcaligenes faecalis T1. The molecular mass of these enzymes were all around 40–50 kDa. Nonionic detergent, diisopropylfluorophosphate and dithiothreitol inhibited the PHB depolymerase activity of all these enzymes. Trypsin abolished PHB depolymerase activity, but not theD-3-hydroxybutyric acid dimer hydrolase activity of all the enzymes. These results showed that the basic properties of these PHB depolymerases resemble those of theA. faecalis T1 enzyme. Analysis ofN-terminal amino acid sequence of the purified enzymes revealed that these enzymes includingA. faecalis T1 enzyme fall into three groups.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02067789
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  • 4
    Electronic Resource
    Electronic Resource
    Effect of limited tryptic modification of a bacterial poly(3-hydroxybutyrate) depolymerase on its catalytic activity
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 952 (1988), S. 164-171 
    Details
    ISSN: 0167-4838
    Keywords: (A. faecalis) ; Poly(3-hydroxybutyrate) ; Poly(3-hydroxybutyrate) depolymerase
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0167-4838(88)90112-4
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  • 5
    Electronic Resource
    Electronic Resource
    Pigments of Rubrobacter radiotolerans (1994)
    Springer
    Archives of microbiology 162 (1994), S. 414-421 
    Details
    ISSN: 1432-072X
    Keywords: Key words     Carotenoid ; Bacterioruberin ; Red pigment ; Radiotolerance ; Rubrobacter radiotolerans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract      The highly radioresistant Rubrobacter radiotolerans, contains red pigments. Since the pigments could not be extracted by usual methods, a new method was developed in which the pigments were extracted with organic solvents after addition of 10 N KOH to the intact cells, followed by neutralization. These pigments were also extracted after treatment with achromopeptidase, but not with lysozyme. The extracted pigments separated into two main spots by TLC (48.6% and 22.6%), and were confirmed to be carotenoids by chemical tests. The two major pigments had 13 conjugated double bonds as determined from the main maximum wavelength of the light absorption spectra. Their molecular weights were determined to be 740 and 722 by mass spectrometry. The mass spectra of their TMS-derivatives revealed that they contained four and three tertiary OH groups, respectively. Confirming their identical light and IR spectra, these pigments were determined to be bacterioruberin and monoanhydrobacterioruberin, respectively, the characteristic carotenoids of halophilic bacteria. The existence of these pigments in bacteria other than halobacteria provides interesting new evidence on the distribution of these compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050159
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  • 6
    Electronic Resource
    Electronic Resource
    Pigments of Rubrobacter radiotolerans (1994)
    Springer
    Archives of microbiology 162 (1994), S. 414-421 
    Details
    ISSN: 1432-072X
    Keywords: Carotenoid ; Bacterioruberin ; Red pigment ; Radiotolerance ; Rubrobacter radiotolerans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The highly radioresistant Rubrobacter radiotolerans, contains red pigments. Since the pigments could not be extracted by usual methods, a new method was developed in which the pigments were extracted with organic solvents after addition of 10 N KOH to the intact cells, followed by neutralization. These pigments were also extracted after treatment with achromopeptidase, but not with lysozyme. The extracted pigments separated into two main spots by TLC (48.6% and 22.6%), and were confirmed to be carotenoids by chemical tests. The two major pigments had 13 conjugated double bonds as determined from the main maximum wavelength of the light absorption spectra. Their molecular weights were determined to be 740 and 722 by mass spectrometry. The mass spectra of their TMS-derivatives revealed that they contained four and three tertiary OH groups, respectively. Confirming their identical light and IR spectra, these pigments were determined to be bacterioruberin and monoanhydrobacterioruberin, respectively, the characteristic carotenoids of halophilic bacteria. The existence of these pigments in bacteria other than halobacteria provides interesting new evidence on the distribution of these compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00282106
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    Paper (German National Licenses)
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  • 7
    Electronic Resource
    Electronic Resource
    cDNA cloning, tissue expression, and chromosome mapping of human homolog of SOX18 (2000)
    Springer
    Journal of human genetics 45 (2000), S. 192-195 
    Details
    ISSN: 1435-232X
    Keywords: Key wordsSOX18 ; HMG-box ; RH mapping ; Chromosome 20q13.33
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The SRY (sex-determining region Y) gene encodes a transcription factor characterized by a DNA-binding motif termed the HMG (high mobility group) domain. The SOX (Sry-box) genes comprise a large family related by homology to the HMG-box region. We isolated a cDNA clone with an open reading frame encoding a putative protein of 384 amino acids, which shared 83% identity to the mouse Sox18 protein. Northern blot analysis revealed that a 1.9-kb band of human SOX18 messenger RNAs was predominantly expressed in heart, although weak signals were seen in brain, liver, testis, and leukocyte. By polymerase chain reaction (PCR)-based analyses with both a human/rodent monochromosomal hybrid cell panel and a radiation hybrid panel, the gene was mapped to the chromosome 20q13.33 region.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s100380050210
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  • 8
    Electronic Resource
    Electronic Resource
    cDNA cloning of a human RAB26-related gene encoding a Ras-like GTP-binding protein on chromosome 16p13.3 region (2000)
    Springer
    Journal of human genetics 45 (2000), S. 309-314 
    Details
    ISSN: 1435-232X
    Keywords: Key words Ras superfamily of small GTP-binding proteins ; RAB26-related ; Rab26 ; RT-PCR ; RH mapping ; Chromosome 16p13.3 ; Virtual transcribed sequence (VTS)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Members of the RAB protein family are important regulators of vesicular fusion and trafficking. A putative new member of the RAB family of genes was identified through a public database search, and its full-length cDNA was isolated from a human fetal brain cDNA library. The predicted protein product of the gene consists of 190 amino acid residues and has 87% identity with rat Rab26. Thus, we designated this gene as the human RAB26-related gene. Reverse transcription-coupled polymerase chain reaction (RT-PCR) demonstrated that the RAB26-related messenger RNA was predominantly expressed in adult and fetal brain. Furthermore, an RT-PCR experiment for brain subregions showed that the mRNA was highly expressed in the amygdala, cerebellum, caudate nucleus, and hippocampus. By PCR-based analysis with both a human/rodent monochromosomal hybrid cell panel and a radiation hybrid panel, the gene was mapped to the chromosome 16p13.3 region between markers WI-7742 and WI-3061. The RAB26-related gene consists of eight exons that span about 44 kb of the genome DNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s100380070023
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  • 9
    Electronic Resource
    Electronic Resource
    Isolation, tissue expression, and chromosomal assignment of a novel human gene which encodes a protein with RING finger motif (1998)
    Springer
    Journal of human genetics 43 (1998), S. 272-274 
    Details
    ISSN: 1435-232X
    Keywords: Key words RING finger ; Full-Length enriched cDNA library ; Chromosome 6p21.3 ; RH mapping
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We identified a novel gene encoding a RING finger (C3HC4-type zinc finger) protein from a human neuroblastoma full-length enriched cDNA library. This cDNA clone consists of 1919 nucleotides with an open reading frame of a 485-amino acid protein. From reverse transcription (RT)-polymerase chain reaction (PCR) analysis, the messenger RNA was ubiquitously expressed in various human adult tissues. The chromosomal location of the gene was determined on the chromosome 6p21.3 region by PCR-based analyses with both a human/rodent monochromosomal hybrid cell panel and a radiation hybrid mapping panel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s100380050088
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  • 10
    Electronic Resource
    Electronic Resource
    cDNA cloning of a novel human gene NAKAP95, neighbor of A-kinase anchoring protein 95 (AKAP95) on chromosome 19p13.11–p13.12 region (2000)
    Springer
    Journal of human genetics 45 (2000), S. 31-37 
    Details
    ISSN: 1435-232X
    Keywords: Key words Cyclic AMP-dependent protein kinase (PKA) ; A-kinase anchoring proteins (AKAPs) ; AKAP95 ; Chromosome 19p13.11–p13.12 ; RH mapping ; Genomic structure ; Gene duplication
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract A-kinase anchoring protein 95 (AKAP95) is a nuclear protein which binds to the regulatory subunit (RII) of cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) and to DNA. A novel nuclear human gene which shares sequence homology with the human AKAP95 gene was identified by a nuclear transportation trap method. By polymerase chain reaction (PCR)-based analysis with both a human/rodent monochromosomal hybrid cell panel and a radiation hybrid panel, the gene was mapped to the chromosome 19p13.11–p13.12 region between markers WI-4669 and CHLC.GATA27C12. Furthermore, alignment with genomic sequences revealed that the gene and human AKAP95 resided tandemly only approximately 250 bp apart from each other. We designated this gene as neighbor of AKAP95 (NAKAP95). The exon-intron structure of NAKAP95 and AKAP95 was conserved, indicating that they may have evolved by gene duplication. The predicted protein product of the NAKAP95 gene consists of 646 amino acid residues, and NAKAP95 and AKAP95 had an overall 40% similarity, both having a potential nuclear localizing signal and two C2H2 type zinc finger motifs. The putative RII binding motif in AKAP95 was not conserved in NAKAP95. A reverse transcription coupled (RT)-PCR experiment revealed that the NAKAP95 gene was transcribed ubiquitously in various human tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s100380070040
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