Source:http://linkedlifedata.com/resource/pubmed/id/19519417
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2009-6-12
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pubmed:abstractText |
In spite of its wide application to protein refolding, purification, and storage, we have not yet addressed a general solution to the mechanism of the effects of arginine hydrochloride on proteins. To elucidate the mechanism of the effects on proteins, several attempts have been reported. In this review, we would review the attempts from thermodynamic and kinetic viewpoints.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1873-4316
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
415-20
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pubmed:meshHeading |
pubmed-meshheading:19519417-Arginine,
pubmed-meshheading:19519417-Binding Sites,
pubmed-meshheading:19519417-Biopharmaceutics,
pubmed-meshheading:19519417-Chemical Fractionation,
pubmed-meshheading:19519417-Multiprotein Complexes,
pubmed-meshheading:19519417-Protein Binding,
pubmed-meshheading:19519417-Proteins,
pubmed-meshheading:19519417-Technology, Pharmaceutical
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pubmed:year |
2009
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pubmed:articleTitle |
To be excluded or to bind, that is the question: Arginine effects on proteins.
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pubmed:affiliation |
Department of Medical Genome Sciences, The University of Tokyo, Kashiwa, Chiba, Japan.
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pubmed:publicationType |
Journal Article,
Review
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