Abstract
Polyethylene glycol modified hemoglobins (PEGHbs) was characterized by liquid chromatography and fluorescence methods. We prepared four samples of two different molecular weight PEG, 5KDa and 20KDa, modified bovine and human hemoglobin. We studied the oxygen affinities, stabilities, and peroxidase activities of PEGHbs. We have related oxygen affinities with different degrees of modifications. The data showed that the modification on the beta subunits was less stable than that of the alpha subunits on the human Hb based samples especially. We also compared peroxidase activities among different modified PEGHbs.http://adsabs.harvard.edu/abs/2011APS..MARJ39010S
| Original language | American English |
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| State | Published - Mar 21 2011 |
| Event | American Physical Society March Meeting - Duration: Mar 21 2011 → … |
Conference
| Conference | American Physical Society March Meeting |
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| Period | 03/21/11 → … |
DC Disciplines
- Physics