Changes in conformation and function of hemoglobin and myoglobin induced by adsorption to silica. |
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| Authors: | B E Hallaway P E Hallaway W A Tisel A Rosenberg |
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| Institution: | Department of Laboratory Medicine and Pathology University of Minnesota, Minneapolis, Minnesota 55455 USA |
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| Abstract: | Adsorption of myoglobin (Mb) or hemoglobin (Hb) to silica (Cab-O-Sil) causes marked alterations in protein hydrogen exchange kinetics. The exchange is slower for cyanometMb and faster for both cyanometHb and oxyHb in adsorbed state than for the corresponding species in the free state. For Hb, adsorption increases oxygen affinity (P50 = 12.9 mmHg vs. 16.7 for free) and decreases cooperativity (n = 2.05 vs. 2.87 for free). Myoglobin has the same oxygen affinity in both the free and adsorbed states. |
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