rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1976-7-6
|
pubmed:abstractText |
Analysis of the time decay of fluorescence anisotropy of 1-dimethylaminoaphthalene-5-sulfonyl (DNS) and fluorescamine derivatives of bovine alpha-lactalbumin and lysozyme reveals that no significant differences in mean rotational relaxation times are present. While fluorescamine molecules appear to orient randomly on these proteins, DNS is bound with a preferential orientation. Other fluorescence characteristics of the labels are also cited.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0301-4622
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
4
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
203-13
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:1260101-Animals,
pubmed-meshheading:1260101-Binding Sites,
pubmed-meshheading:1260101-Cattle,
pubmed-meshheading:1260101-Dansyl Compounds,
pubmed-meshheading:1260101-Fluorescamine,
pubmed-meshheading:1260101-Lactalbumin,
pubmed-meshheading:1260101-Mathematics,
pubmed-meshheading:1260101-Muramidase,
pubmed-meshheading:1260101-Protein Binding,
pubmed-meshheading:1260101-Protein Conformation,
pubmed-meshheading:1260101-Spectrometry, Fluorescence,
pubmed-meshheading:1260101-Time Factors
|
pubmed:year |
1976
|
pubmed:articleTitle |
A comparative study on bovine alpha-lactalbumin and lysozyme by nanosecond fluorometry.
|
pubmed:publicationType |
Journal Article,
Comparative Study
|