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 of 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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