ライフサイエンスコーパス: hemichrome

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1 oxidation of hemoglobin to methemoglobin and hemichrome.

2 igh ratio of an anionic form of bishistidine hemichrome.

3 oglobin, p72syk protein tyrosine kinase, and hemichromes.

4 In contrast to free Fe(III) alphaHb hemichromes, AHSP-bound Fe(III) alphaHb does not precipi

5 proposes that denatured/oxidized hemoglobin (hemichromes) arising late during an RBC's life span indu

6 ages and were free to cluster in response to hemichrome binding.

7 molecule are the axial heme ligands, to the hemichrome (bishistidine) form, in which the proximal hi

8 ted AHSPs drive the formation of a met-alpha hemichrome conformation following binding to either met-

9 s an apoglobin (apo-rHb), a non-cross-linked hemichrome (ferric iron and histidine axial ligands, rHb

10 by rapidly binding and stabilizing met-alpha hemichrome folding intermediates.

11 rdinate hemin (Fe(III)-protoporphyrin IX) or hemichrome form (hemiHtsA) with an apparent rate constan

12 The steps proximate to hemichrome formation in these cells are poorly understoo

13 esults suggest possible functional roles for hemichrome formation in vivo.

14 Hemichrome formation is coupled to a large tertiary stru

15 s procedure resulted in a protein with fewer hemichrome impurities than was obtained by an overexpres

16 e detrimental formation of methemoglobin and hemichrome in vivo, insofar as this is accelerated by tr

17 this intermediate oxidizes to form a stable hemichrome in which the proximal (F8) and distal (E7) hi

18 The predominant myoglobin hemichrome is a chemically reversible dihistidyl complex

19 Abnormal deposition of hemichrome on the inner aspect of the sickle red cell me

20 ve of hemoglobin oxidation and deposition of hemichrome on the membrane.

21 ne axial ligands, rHb-R), and a cross-linked hemichrome (rHb-A).

22 o be a simple two-state process, even though hemichrome spectra are often observed and apoMb denatura

23 ded intermediate with hemin bound (IH) has a hemichrome spectrum indicative of a bis-histidyl axial c

24 orm causes the formation of a characteristic hemichrome spectrum with a maximum at 565 nm and a shoul

25 nversion to a partially unfolded bishistidyl hemichrome structure.

26 exhibit spectral features characteristic of hemichrome-type signals.

27 rosylmyoglobin produces low-spin ferric heme hemichromes which have been characterized by electron sp

28 and convert ferrous/ferric haem proteins to hemichromes with a unique absorption peak at 535 nm.

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