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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
1997-1-31
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pubmed:abstractText |
The complete amino acid sequence of the A chain of mistletoe lectin I was determined via Edman degradation sequencing of the N-terminus and tryptic and endoproteinase Asp-N overlapping fragments, amino acid analysis and MALDI-MS. The data obtained show a great homology with the chains of ribosome-inactivating proteins such as ricin and abrin with 111 (abrin-a) and 103 (ricin-D) amino acid residues conserved, respectively. The knowledge of the primary structure of MLA will have a fundamental impact on elucidating the biological function of medically applied mistletoe lectins on a molecular basis.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
399
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
153-7
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8980141-Amino Acid Sequence,
pubmed-meshheading:8980141-Lectins,
pubmed-meshheading:8980141-Mistletoe,
pubmed-meshheading:8980141-Molecular Sequence Data,
pubmed-meshheading:8980141-Peptide Fragments,
pubmed-meshheading:8980141-Plant Lectins,
pubmed-meshheading:8980141-Plant Preparations,
pubmed-meshheading:8980141-Plant Proteins,
pubmed-meshheading:8980141-Plants, Medicinal,
pubmed-meshheading:8980141-Ribosome Inactivating Proteins, Type 2,
pubmed-meshheading:8980141-Sequence Homology, Amino Acid,
pubmed-meshheading:8980141-Toxins, Biological
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pubmed:year |
1996
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pubmed:articleTitle |
Complete amino acid sequence of the A chain of mistletoe lectin I.
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pubmed:affiliation |
Abteilung für Physikalische Biochemie des Physiologisch-chemischen Instituts der Universität Tübingen, Germany.
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pubmed:publicationType |
Journal Article
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