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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1984-7-13
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pubmed:abstractText |
Mild treatment of iron-saturated human lactotransferrin by trypsin at pH 8.2 cleaves the molecule into a N-tryptic (Mr approximately equal to 30000) and a C-tryptic (Mr approximately equal to 50000) fragment, which have been isolated. Each of them carries a glycan moiety and keeps the property to bind reversibly one Fe3+. The N-tryptic fragment has been submitted to a second tryptic digestion which led to an iron-binding glycopeptide fragment with a molecular weight of about 18500. This fragment, the smallest iron-binding peptide isolated up to now from a transferrin, includes the ND2 domain of human lactotransferrin.
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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 |
May
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
787
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
90-6
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:6722176-Carbohydrates,
pubmed-meshheading:6722176-Glycopeptides,
pubmed-meshheading:6722176-Humans,
pubmed-meshheading:6722176-Iron,
pubmed-meshheading:6722176-Kinetics,
pubmed-meshheading:6722176-Lactoferrin,
pubmed-meshheading:6722176-Lactoglobulins,
pubmed-meshheading:6722176-Molecular Weight,
pubmed-meshheading:6722176-Peptide Fragments,
pubmed-meshheading:6722176-Spectrophotometry,
pubmed-meshheading:6722176-Trypsin
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pubmed:year |
1984
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pubmed:articleTitle |
Characterization and localization of an iron-binding 18-kDa glycopeptide isolated from the N-terminal half of human lactotransferrin.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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