Erythrocyte stability under imposed fields

1990 ◽  
Vol 15 (3) ◽  
pp. 135-141
Author(s):  
V. Sitaramam
Keyword(s):  
Erythrocyte Stability

Pycnogenol® supplementation improved the erythrocyte stability of packed donkeys during the late hot-dry season in Zaria, Nigeria

2018 ◽  
Vol 28 (2) ◽  
pp. 281-286 ◽  
Author(s):  
Folashade Helen Olaifa ◽  
Ayo Joseph Olusegun ◽  
Aluwong Tangang ◽  
Rekwot Peter Ibrahim ◽  
Friday Ocheja Zakari
Keyword(s):  
Dry Season ◽  
Hot Dry Season ◽  
Erythrocyte Stability

Zinc, iron, vitamin E, and erythrocyte stability in the rat

1989 ◽  
Vol 23 (1) ◽  
pp. 89-96 ◽  
Author(s):  
Ian R. Record ◽  
Sally E. MacQueen ◽  
Ivor E. Dreosti
Keyword(s):  
Vitamin E ◽  
Erythrocyte Stability

scholarly journals The structure of the ankyrin-binding site of β-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties

Blood ◽  
2009 ◽  
Vol 113 (22) ◽  
pp. 5377-5384 ◽  
Author(s):  
Paul R. Stabach ◽  
Ivana Simonović ◽  
Miranda A. Ranieri ◽  
Michael S. Aboodi ◽  
Thomas A. Steitz ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Protein Targeting ◽  
Repeat Unit ◽  
Structural Constraints ◽  
Relative Positioning ◽  
Binding Properties ◽  
Repeat Structure ◽  
Erythrocyte Stability ◽  
Spectrin Repeats ◽  
Specific Ligand

Spectrin and ankyrin participate in membrane organization, stability, signal transduction, and protein targeting; their interaction is critical for erythrocyte stability. Repeats 14 and 15 of βI-spectrin are crucial for ankyrin recognition, yet the way spectrin binds ankyrin while preserving its repeat structure is unknown. We have solved the crystal structure of the βI-spectrin 14,15 di-repeat unit to 2.1 Å resolution and found 14 residues critical for ankyrin binding that map to the end of the helix C of repeat 14, the linker region, and the B-C loop of repeat 15. The tilt (64°) across the 14,15 linker is greater than in any published di-repeat structure, suggesting that the relative positioning of the two repeats is important for ankyrin binding. We propose that a lack of structural constraints on linker and inter-helix loops allows proteins containing spectrin-like di-repeats to evolve diverse but specific ligand-recognition sites without compromising the structure of the repeat unit. The linker regions between repeats are thus critical determinants of both spectrin's flexibility and polyfunctionality. The putative coupling of flexibility and ligand binding suggests a mechanism by which spectrin might participate in mechanosensory regulation.

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