Albinism

Research from Baylor College of Medicine, College of Medicine provide new insights into life sciences

Albinism Library Library Home This article was published in Hematology Week, which you can subscribe to online.

"SDS can convert inactive PO and the oxygen carrier hemocyanin (Hc) into enzymatically active PO. Here we present single-particle cryo-EM maps at subnanometer resolution and pseudoatomic models of the 24-oligomeric Hc from scorpion Pandinus imperator in resting and SDS-activated states. Our structural analyses led to a plausible mechanism of Hc enzyme PO activation: upon SDS activation, the intrinsically flexible Hc domain I twists away from domains II and III in each subunit, exposing the entrance to the active site; this movement is stabilized by enhanced interhexamer and interdodecamer interactions, particularly in the central linker subunits," wrote Y. Cong and colleagues, Baylor College of Medicine, College of Medicine.

The researchers concluded: "This mechanism could be applicable to other type 3 copper proteins, as the active site is highly conserved."

Cong and colleagues published the results of their research in Structure (Structural Mechanism of SDS-Induced Enzyme Activity of Scorpion Hemocyanin Revealed by Electron Cryomicroscopy. Structure, 2009;17(5):749-758).

For additional information, contact W. Chiu, Baylor College of Medicine, National Center Macromolecular Imaging, Houston, TX 77030, USA.

The publisher of the journal Structure can be contacted at: Cell Press, 600 Technology Square, 5TH Floor, Cambridge, MA 02139, USA.

Keywords: United States, Houston, Life Sciences, Oxygen Carrier, Blood Transfusion, Blood Substitutes, Medical Device, Transfusion Medicine, Artificial Blood, Biomedical Engineering, Bioengineering, Biomedicine, Albinism, Melanoma, Enzymology, Microscopy, Baylor College of Medicine, College of Medicine.

This article was prepared by Hematology Week editors from staff and other reports. Copyright 2009, Hematology Week via NewsRx.com.