Article
Sickle hemoglobin polymer stability probed by triple and quadruple mutant hybrids.
The Journal of biological chemistry - 19 Apr 2002
Li Xianfeng, Briehl Robin W, Bookchin Robert M, Josephs Robert, Wei Baoyang, Manning James M, Ferrone Frank A
Abstract excerpt
As part of an effort to understand the interactions in HbS polymerization, we have produced and studied a recombinant triple mutant, D6A(alpha)/D75Y(alpha)/E121R(beta), and a quadruple mutant comprising the preceding mutation plus the natural genetic mutation of sickle hemoglobin, E6V(beta). These recombinant hemoglobins expressed in yeast were extensively characterized, and their structure and oxygen binding...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
