1997
DOI: 10.1093/clinchem/43.9.1796
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Evaluation of HemogloBind™ for Removal of o-Raffinose Cross-Linked Hemoglobin (Hemolink™) from Serum

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Cited by 8 publications
(2 citation statements)
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“…HemogloBind binds Hb unspecifically by a combination of its polymer composition, charge properties and cross-linking architecture [23]. Apparently, the physiochemical properties of Hb and Hb-Hp causes HemogloBind to preferentially bind Hb and not Hb-Hp, as shown in western blots of HemogloBind-treated plasma samples and also reported previously [24].…”
Section: Discussionsupporting
confidence: 58%
“…HemogloBind binds Hb unspecifically by a combination of its polymer composition, charge properties and cross-linking architecture [23]. Apparently, the physiochemical properties of Hb and Hb-Hp causes HemogloBind to preferentially bind Hb and not Hb-Hp, as shown in western blots of HemogloBind-treated plasma samples and also reported previously [24].…”
Section: Discussionsupporting
confidence: 58%
“…Thus, we focused on aldehydes with a small molecular weight. Such aldehydes readily diffuse in solution and show high reactivity with amino groups in proteins, even under physiological condition . We therefore considered that a small molecule containing multiple aldehyde groups could efficiently crosslink atelocollagen molecules dissolved in physiological saline.…”
Section: Resultsmentioning
confidence: 99%