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Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Bluard-Deconinck, JM | - |
dc.contributor.author | Williams, J | - |
dc.contributor.author | Evans, RW | - |
dc.contributor.author | Snick, JV | - |
dc.contributor.author | Osinski, PA | - |
dc.contributor.author | Massont, PL | - |
dc.date.accessioned | 2010-05-13T11:30:59Z | - |
dc.date.available | 2010-05-13T11:30:59Z | - |
dc.date.issued | 1978 | - |
dc.identifier.citation | Biochemical Journal. 171: 321-327 | en |
dc.identifier.issn | 0264-6021 | - |
dc.identifier.uri | http://bura.brunel.ac.uk/handle/2438/4338 | - |
dc.description.abstract | Digestion of lactoferrin with pepsin at pH 3.0 gave an iron-binding half-molecule that represents the C-terminal part of the native protein. Tryptic or chymotryptic digestion of 30%/-iron-saturated lactoferrin yielded the N- and C-terminal half molecules, which could be separated by DEAE-Sephadex chromatography. The N- and C-terminal fragments did not show any immunological cross-reaction. The carbohydrate of lactoferrin was distributed equally between the two fragments. | en |
dc.language.iso | en | en |
dc.publisher | Portland Press | en |
dc.title | Iron-binding fragments from the N-Terminal and C-Terminal regions of human lactoferrin | en |
dc.type | Article | en |
Appears in Collections: | Biological Sciences Dept of Life Sciences Research Papers |
Files in This Item:
File | Description | Size | Format | |
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biochem-1978.pdf | 1.04 MB | Adobe PDF | View/Open |
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