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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Mechanism of autolysis of Neisseria gonorrhoeae.</title>
<author><name sortKey="Hebeler, B H" sort="Hebeler, B H" uniqKey="Hebeler B" first="B H" last="Hebeler">B H Hebeler</name>
</author>
<author><name sortKey="Young, F E" sort="Young, F E" uniqKey="Young F" first="F E" last="Young">F E Young</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PMC</idno>
<idno type="pmid">7545</idno>
<idno type="pmc">233143</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC233143</idno>
<idno type="RBID">PMC:233143</idno>
<date when="1976">1976</date>
<idno type="wicri:Area/Pmc/Corpus">000049</idno>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Mechanism of autolysis of Neisseria gonorrhoeae.</title>
<author><name sortKey="Hebeler, B H" sort="Hebeler, B H" uniqKey="Hebeler B" first="B H" last="Hebeler">B H Hebeler</name>
</author>
<author><name sortKey="Young, F E" sort="Young, F E" uniqKey="Young F" first="F E" last="Young">F E Young</name>
</author>
</analytic>
<series><title level="j">Journal of Bacteriology</title>
<idno type="ISSN">0021-9193</idno>
<idno type="eISSN">1098-5530</idno>
<imprint><date when="1976">1976</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>The major autolysin(s) of Neisseria gonorrhoeae was solubilized from envelopes by extraction with 2% Triton X-100 containing 0.5 M NaCl. Neither Triton X-100 nor NaCl alone could effectively release the autolysin(s). The major autolysin is N-acetylmuramyl-L-alanine amidase (EC 3.5.1.28). The pH optimum for this reaction was broad, ranging from 5.5 to 8.5. Optimal hydrolysis of peptidoglycan occurred in 2% Triton X-100 in 0.1 M KCl. Attempts to purify the autolysin were unsuccessful. A rapid assay for enzyme activity was developed using radioactive cell walls as a substrate ([3H]diaminopimelic acid).</p>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Bacteriol</journal-id>
<journal-title>Journal of Bacteriology</journal-title>
<issn pub-type="ppub">0021-9193</issn>
<issn pub-type="epub">1098-5530</issn>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">7545</article-id>
<article-id pub-id-type="pmc">233143</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Mechanism of autolysis of Neisseria gonorrhoeae.</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Hebeler</surname>
<given-names>B H</given-names>
</name>
</contrib>
<contrib contrib-type="author"><name><surname>Young</surname>
<given-names>F E</given-names>
</name>
</contrib>
</contrib-group>
<pub-date pub-type="ppub"><month>6</month>
<year>1976</year>
</pub-date>
<volume>126</volume>
<issue>3</issue>
<fpage>1186</fpage>
<lpage>1193</lpage>
<abstract><p>The major autolysin(s) of Neisseria gonorrhoeae was solubilized from envelopes by extraction with 2% Triton X-100 containing 0.5 M NaCl. Neither Triton X-100 nor NaCl alone could effectively release the autolysin(s). The major autolysin is N-acetylmuramyl-L-alanine amidase (EC 3.5.1.28). The pH optimum for this reaction was broad, ranging from 5.5 to 8.5. Optimal hydrolysis of peptidoglycan occurred in 2% Triton X-100 in 0.1 M KCl. Attempts to purify the autolysin were unsuccessful. A rapid assay for enzyme activity was developed using radioactive cell walls as a substrate ([3H]diaminopimelic acid).</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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