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        <identifier>oai:www.ideals.illinois.edu:2142/71780</identifier>
        <datestamp>2023-07-11</datestamp>
        <setSpec>col_2142_5131</setSpec>
        <setSpec>col_2142_47040</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>Yoo, Won-Hyung</dc:creator>
          <dc:date>2014-12-16T20:45:13Z</dc:date>
          <dc:date>2014-12-16T20:45:13Z</dc:date>
          <dc:date>10000-01-01</dc:date>
          <dc:date>1985</dc:date>
          <dc:date>1985</dc:date>
          <dc:description>This study was undertaken to elucidate into the mode of accumulation and subsequent degradation of storage proteins in apple trees. Protein isolation, characterization, and proteolytic enzyme study were involved.</dc:description>
          <dc:description>The prominent proteins present in shoot bark were the MWs 56, 38, 28, and 20 kD. These 4 proteins constituted a high proportion of the total protein in bark increasing from 46 to 70% of the total protein during senescence. The 4 major proteins appeared to serve a storage role and consisted of many heterogeneous polypeptides of different isoelectric points. Twenty one, thirteen, seven, and twenty one heterogeneous polypeptides were found in those 4 major proteins, respectively. Each of the 4 major proteins had similar amino acid composition in their hydrolysates with approximately 40% of the total protein in basic amino acids, asparagine, glutamine, and their amides. The highest proteolytic activity was found when the 20 kD protein were used as a substrate.</dc:description>
          <dc:description>During regrowth, a slightly greater degradation of the four dominant proteins was observed. A preferential degradation of some bark proteins differing in electrical charges was also found. Nonetheless, the protein degradation was not limited to a few protein species.</dc:description>
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8600356.pdf: 3214036 bytes, checksum: d62e1e3e747478a941692e8abecbf636 (MD5)
  Previous issue date: 1985</dc:description>
          <dc:description>Embargo set by: Seth Robbins for item 71946
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>118 p.</dc:description>
          <dc:description>Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 1985.</dc:description>
          <dc:identifier>http://hdl.handle.net/2142/71780</dc:identifier>
          <dc:identifier>(UMI)AAI8600356</dc:identifier>
          <dc:subject>Biology, Plant Physiology</dc:subject>
          <dc:title>Storage Proteins in Apple Trees (Woody Plant, Nitrogen, Senescence)</dc:title>
          <dc:type>text</dc:type>
          <degree>
            <department>Horticulture</department>
            <discipline>Horticulture</discipline>
            <grantor>University of Illinois at Urbana-Champaign</grantor>
            <level>Dissertation</level>
            <name>Ph.D.</name>
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