| DOI | Resolve DOI: https://doi.org/10.1016/0009-2614(89)85188-7 |
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| Author | Search for: Szabo, A.1; Search for: Willis, K.; Search for: Krajcarski, D.1; Search for: Alpert, B. |
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| Affiliation | - National Research Council Canada. NRC Institute for Biological Sciences
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| Format | Text, Article |
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| Abstract | Nanosecond fluorescence lifetime components, observed in hemoglobin samples purified by standard procedures, are removed by a HPLC purification step. The tryptophyl fluorescence of extensively purified human hemoglobin is found to decay as a simple single exponential. The fluorescence lifetime of ≈25 ps is relatively insensitive to protein conformational changes such as those resulting from different ligation states of the heme iron. |
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| Publication date | 1989-11 |
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| Publisher | Elsevier |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | SZABO1989 |
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| NPARC number | 9365238 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 03ef3dcc-b3cc-4346-8722-83fec9c4c279 |
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| Record created | 2009-07-10 |
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| Record modified | 2020-03-17 |
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