The preparation and use of biotinylated trypsin in western blotting for the detection of trypsin inhibitory proteins
- Publisher:
- Academic Press Inc Jnl-Comp Subscriptions
- Publication Type:
- Journal Article
- Citation:
- Analytical Biochemistry, 1994, 222 (1), pp. 34 - 43
- Issue Date:
- 1994-01
Closed Access
Full metadata record
Field | Value | Language |
---|---|---|
dc.contributor.author | Melrose, J | en_US |
dc.contributor.author | Rodgers, K | en_US |
dc.contributor.author | Ghosh, P | en_US |
dc.date.issued | 1994-01 | en_US |
dc.identifier.citation | Analytical Biochemistry, 1994, 222 (1), pp. 34 - 43 | en_US |
dc.identifier.issn | 0003-2697 | en_US |
dc.identifier.uri | http://hdl.handle.net/10453/14667 | |
dc.description.abstract | Methods were developed for the preparation of biotinylated trypsin of high specific activity. This was used as a probe for the detection of serine proteinase inhibitory proteins which had been separated by sodium dodecyl sulfate-polyacrylamide gradient s | en_US |
dc.format | Scott McWhirter | en_US |
dc.publisher | Academic Press Inc Jnl-Comp Subscriptions | en_US |
dc.relation.ispartof | Analytical Biochemistry | en_US |
dc.relation.isbasedon | 10.1006/abio.1994.1450 | en_US |
dc.subject.classification | Biochemistry & Molecular Biology | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Cattle | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Biotin | en_US |
dc.subject.mesh | Trypsin | en_US |
dc.subject.mesh | Trypsin Inhibitors | en_US |
dc.subject.mesh | Blotting, Western | en_US |
dc.subject.mesh | Electrophoresis, Polyacrylamide Gel | en_US |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Biotin | en_US |
dc.subject.mesh | Blotting, Western | en_US |
dc.subject.mesh | Cattle | en_US |
dc.subject.mesh | Electrophoresis, Polyacrylamide Gel | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Trypsin | en_US |
dc.subject.mesh | Trypsin Inhibitors | en_US |
dc.title | The preparation and use of biotinylated trypsin in western blotting for the detection of trypsin inhibitory proteins | en_US |
dc.type | Journal Article | |
utslib.citation.volume | 1 | en_US |
utslib.citation.volume | 222 | en_US |
utslib.location.activity | ISI:A1994PM43900006 | en_US |
utslib.for | 0601 Biochemistry and Cell Biology | en_US |
utslib.for | 0301 Analytical Chemistry | en_US |
utslib.for | 0301 Analytical Chemistry | en_US |
utslib.for | 0601 Biochemistry And Cell Biology | en_US |
utslib.for | 0399 Other Chemical Sciences | en_US |
dc.location.activity | ISI:A1994PM43900006 | en_US |
dc.location.activity | ISI:A1994PM43900006 | |
pubs.embargo.period | Not known | en_US |
pubs.organisational-group | /University of Technology Sydney | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
pubs.organisational-group | /University of Technology Sydney/Faculty of Science/School of Life Sciences | |
pubs.organisational-group | /University of Technology Sydney/Strength - CHT - Health Technologies | |
utslib.copyright.status | closed_access | |
pubs.consider-herdc | false | en_US |
pubs.issue | 1 | en_US |
pubs.notes | Ok-SAM | en_US |
pubs.volume | 222 | en_US |
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Filename | Description | Size | |||
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![]() | 2010000603OK.pdf | 1.03 MB | Adobe PDF |
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Abstract:
Methods were developed for the preparation of biotinylated trypsin of high specific activity. This was used as a probe for the detection of serine proteinase inhibitory proteins which had been separated by sodium dodecyl sulfate-polyacrylamide gradient s
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