Ontology highlight
ABSTRACT:
SUBMITTER: Brillet T
PROVIDER: S-EPMC2878560 | biostudies-literature | 2010 Jun
REPOSITORIES: biostudies-literature
Brillet Thomas T Baudin-Creuza Véronique V Vasseur Corinne C Domingues-Hamdi Elisa E Kiger Laurent L Wajcman Henri H Pissard Serge S Marden Michael C MC
The Journal of biological chemistry 20100406 23
A kinetic analysis has been made of the interaction of alpha-Hb chains with a mutant alpha-hemoglobin stabilizing protein, AHSP(V56G), which is the first case of an AHSP mutation associated with clinical symptoms of mild thalassemia syndrome. The chaperone AHSP is thought to protect nascent alpha chains until final binding to the partner beta-Hb. Rather than protecting alpha chains, the mutant chaperone is partially unfolded but recovers its secondary structure via interaction with alpha-Hb. For ...[more]