WordNet

a colorless protein obtained by removing heme from hemoglobin; the oxygen carrying compound in red blood cells (同)hematohiston, haematohiston

English Journal

Novel surface plasmon resonance sensor for the detection of heme at biological levels via highly selective recognition by apo-hemoglobin.

Briand VA, Thilakarathne V, Kasi RM, Kumar CV.SourceDepartment of Chemistry, University of Connecticut Storrs, CT 06269 3060, USA.
Talanta.Talanta.2012 Sep 15;99:113-8. doi: 10.1016/j.talanta.2012.05.026. Epub 2012 May 25.
We have developed a novel surface plasmon resonance (SPR) biosensor for heme detection that utilizes the reconstitution of the heme cofactor with apohemoglobin (apoHb), hemoglobin from which the heme has been removed, as the sensing mechanism. The binding is highly specific, efficient and generated
PMID 22967529

AHSP (α-haemoglobin-stabilizing protein) stabilizes apo-α-haemoglobin in a partially folded state.

Krishna Kumar K, Dickson CF, Weiss MJ, Mackay JP, Gell DA.SourceSchool of Molecular Bioscience, University of Sydney, Sydney, NSW 2006, Australia.
The Biochemical journal.Biochem J.2010 Dec 1;432(2):275-82. doi: 10.1042/BJ20100642.
To produce functional Hb (haemoglobin), nascent α-globin (αo) and β-globin (βo) chains must each bind a single haem molecule (to form αh and βh) and interact together to form heterodimers. The precise sequence of binding events is unknown, and it has been suggested that additional factors migh
PMID 20860551

[The mechanisms of the proteolytic degradation of native globular proteins. The role of local and global fluctuations of the native structure].

Abaturov LV, Burshteĭn EA, Nosova NG.AbstractAnalysis of the proteolytic degradation of the native protein structure carried out by the comparison of the temperature dependence of the hydrogen exchange and proteolytic splitting rates of the hen egg-white lysozyme and human Hb and apoHb. Acceleration of the burst-like (all or none) proteolytic degradation in the high temperature range is provided by the intensification of the global fluctuations with overall unfolding revealed by hydrogen exchange. For Hb and apoHb the rate of burst-like proteolytic degradation and hydrogen exchange weakly depends on temperature in the range, where hydrogen exchange reveals only local fluctuations of the native protein structure. The splitting of the two proteins proceeds by the selfaccelerated burst-like mechanism with the initial rate-limiting single cleavage owing to the local fluctuation of the native structure. The local fluctuations play important role also upon the intracellular burst-like degradation of native proteins.
Molekuliarnaia biologiia.Mol Biol (Mosk).2008 Mar-Apr;42(2):327-40.
Analysis of the proteolytic degradation of the native protein structure carried out by the comparison of the temperature dependence of the hydrogen exchange and proteolytic splitting rates of the hen egg-white lysozyme and human Hb and apoHb. Acceleration of the burst-like (all or none) proteolytic
PMID 18610842

States of Amino Acid Residues in Proteins:XXII. Effect of Cyanide on the Reactivities of Histidine and Tyrosine Residues in Ferrihemoglobin and Ferrimyoglobin