Pub. Date : 2009 Jul
PMID : 18984910
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | In this study, we employed a LC-MS/MS assay to demonstrate that residues 38-51 of apoC-I are significantly protected from proteolysis in the presence of 1,2-dimyristoyl-3-sn-glycero-phosphocholine (DMPC). | Dimyristoylphosphatidylcholine | apolipoprotein C1 | Homo sapiens |
2 | In contrast to wild-type apoC-I (WT), which binds DMPC vesicles with an apparent Kd [Kd(app)] of 0.89 microM, apoC-I(F42A) and apoC-I(F46A) possess 2-fold weaker affinities for DMPC with Kd(app) of 1.52 microM and 1.58 microM, respectively. | Dimyristoylphosphatidylcholine | apolipoprotein C1 | Homo sapiens |
3 | In contrast to wild-type apoC-I (WT), which binds DMPC vesicles with an apparent Kd [Kd(app)] of 0.89 microM, apoC-I(F42A) and apoC-I(F46A) possess 2-fold weaker affinities for DMPC with Kd(app) of 1.52 microM and 1.58 microM, respectively. | Dimyristoylphosphatidylcholine | apolipoprotein C1 | Homo sapiens |
4 | However, apoC-I(F46G), apoC-I(F42A/F46A), apoC-I(F42G), and apoC-I(F42G/F46G) bind significantly weaker to DMPC with Kd(app) of 2.24 microM, 3.07 microM, 4.24 microM, and 10.1 microM, respectively. | Dimyristoylphosphatidylcholine | apolipoprotein C1 | Homo sapiens |
5 | However, apoC-I(F46G), apoC-I(F42A/F46A), apoC-I(F42G), and apoC-I(F42G/F46G) bind significantly weaker to DMPC with Kd(app) of 2.24 microM, 3.07 microM, 4.24 microM, and 10.1 microM, respectively. | Dimyristoylphosphatidylcholine | apolipoprotein C1 | Homo sapiens |
6 | However, apoC-I(F46G), apoC-I(F42A/F46A), apoC-I(F42G), and apoC-I(F42G/F46G) bind significantly weaker to DMPC with Kd(app) of 2.24 microM, 3.07 microM, 4.24 microM, and 10.1 microM, respectively. | Dimyristoylphosphatidylcholine | apolipoprotein C1 | Homo sapiens |
7 | However, apoC-I(F46G), apoC-I(F42A/F46A), apoC-I(F42G), and apoC-I(F42G/F46G) bind significantly weaker to DMPC with Kd(app) of 2.24 microM, 3.07 microM, 4.24 microM, and 10.1 microM, respectively. | Dimyristoylphosphatidylcholine | apolipoprotein C1 | Homo sapiens |
8 | Sedimentation velocity studies subsequently show that the protein/DMPC complexes formed by these apoC-I mutants sediment at 6.5S, 6.7S, 6.5S, and 8.0S, respectively. | Dimyristoylphosphatidylcholine | apolipoprotein C1 | Homo sapiens |