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      <header>
        <identifier>oai:www.ideals.illinois.edu:2142/71156</identifier>
        <datestamp>2023-07-11</datestamp>
        <setSpec>col_2142_5131</setSpec>
        <setSpec>col_2142_16338</setSpec>
        <setSpec>com_2142_5130</setSpec>
        <setSpec>com_2142_16337</setSpec>
        <setSpec>com_2142_14793</setSpec>
        <setSpec>com_2142_8903</setSpec>
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        <thesis xmlns="http://www.ndltd.org/standards/metadata/etdms/1.1/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:dc="http://purl.org/dc/elements/1.1/" xsi:schemaLocation="http://www.ndltd.org/standards/metadata/etdms/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdms11.xsd http://purl.org/dc/elements/1.1/ http://www.ndltd.org/standards/metadata/etdms/1.1/etdmsdc.xsd">
          <dc:creator>Tanner, Ralph S.</dc:creator>
          <dc:date>2014-12-16T06:12:48Z</dc:date>
          <dc:date>2014-12-16T06:12:48Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>1982</dc:date>
          <dc:date>1982</dc:date>
          <dc:description>An enzymic assay for the detection and quantitation of component B based on cell-free extract of Methanobacterium thermoautotrophicum stripped of small molecular weight cofactors by anaerobic column chromatography was developed. Component B was purified to homogeneity from boiled cell extract of M. thermoautotrophicum by anaerobic chromatography on Sephadex DEAE-A25, Sephadex G10, and Sephadex G25-F columns. Component B was determined to have a molecular weight of 1,044 by fast atom bombardment mass spectrometry, and a molecular formula of C(,32)H(,47)N(,3)O(,26)P(,2)Na(,4) was proposed for the sodium salt of the compound. A primary amine was present in component B, but no amino acid was detected. Component B was determined to have a monoester phosphate and a diester phosphate, and one mol of aldopentose per mol of component B. The UV absorbance spectrum revealed the presence of two absorbance peaks in component B: one at 267 nm and the other at 233 nm. It was concluded that component B contained a nucleotide moiety.</dc:description>
          <dc:description>The function of component B was not determined. Cyanocobalamin was found to greatly stimulate methylreductase activity in the component B assay system, but the cause of the stimulation was not determined.</dc:description>
          <dc:description>A defined medium was developed for Methanomicrobium mobile; this made possible the study of mobile factor, which is required for the growth of M. mobile. M. mobile was found to require acetate, isobutyrate, 2-methylbutyrate, isovalerate, tryptophan, para-aminobenzoic acid, pyridoxine, thiamine, biotin, and vitamin B(,12) for its growth. Sources of the branched-chain amino acids would not substitute for the branched-chain volatile fatty acids. Indole would substitute for tryptophan, but skatole, anthranilic acid, shikimic acid, or 3-indolelactic acid could not substitute. Folic acid could not substitute for para-aminobenzoic acid. Mobile factor was partially purified by anaerobic chromatography on a Sephadex DEAE-A25 column and a Dowex 50W-X4 column.</dc:description>
          <dc:description>Made available in DSpace on 2014-12-16T06:12:48Z (GMT). No. of bitstreams: 1
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  Previous issue date: 1982</dc:description>
          <dc:description>Embargo set by: Seth Robbins for item 71322
Lift date: Forever
Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs</dc:description>
          <dc:description>U of I Only</dc:description>
          <dc:description>106 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1982.</dc:description>
          <dc:identifier>http://hdl.handle.net/2142/71156</dc:identifier>
          <dc:identifier>(UMI)AAI8303004</dc:identifier>
          <dc:subject>Biology, Microbiology</dc:subject>
          <dc:title>Novel Compounds From Methanogens: Characterization of Component B of the Methylreductase System and Mobile Factor</dc:title>
          <dc:type>text</dc:type>
          <degree>
            <department>Microbiology</department>
            <discipline>Microbiology</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
          </degree>
        </thesis>
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