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KMID : 0578319920020010075
Molecules and Cells
1992 Volume.2 No. 1 p.75 ~ p.81
Interaction of Oxymuoglobin and Apomyoglobin with Phospholipid Vesicles at Low pH
Choi, Young Ho
Lee, Jong Woo/Kim, Hyoungman
Abstract
The binding of sperm whale oxymyoglobin and apomyoglobin to the phosphatidylcholine vesicles and phosphatidylcholine/phosphatidylserine (4:1) mixed vesicles was studied as a function of pH and ionic strength. The binding properties of oxymyoglobin and apomyoglobin were found to be quite different. For oxymyoglobin, the extent of binding increased with decreasing pH, while a reverse pattern was observed for the apomyoglobin. However, an identical segment of oxymyoglobin and apomyoglobin was found to be protected from tryptic digestion of the protein/vesicle complex. The amino acid composition of this segment corresponds to the sequence from N-terminal (Val) to Lys-42. The possible insertion of an N-terminal segment into a vesicle bilayer is discussed in terms of the structure of myoglobin at low pH.
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