Fig. 2: Gly17 on hemoglobin acts as a crucial interaction site for ligand-receptor binding.
From: Hemoglobin in the blood acts as a chemosensory signal via the mouse vomeronasal system
a Types of hemoglobin in BALB/c and C57BL/6 strain blood cell lysate. Two types of hemoglobin (β-globin) in the BALB/c mouse strain were separated by HPLC with a DEAE column. b Number of c-Fos-positive cells in the M/T cell layer of the AOB sections from male mice stimulated with hemoglobin from BALB/c and C57BL/6 male mice blood and blood from various kinds of vertebrates. n = 6 for C57BL/6, Rat, Horse, Human, Guinea pig, Frog, and Zebrafish, n = 8 for BALB/c-major, and n = 9 for BALB/c-minor. Error bars, S.E.M. c Alignment of β-globin amino acid sequences. An amino acid G17 is different in BALB/c minor, horse, frog, and zebrafish β-globin. d Representative immunohistochemical images of total c-Fos-positive cells in the M/T of the AOB sections from G17A-mutant-, H78N-mutant-, and control buffer-stimulated male mice. n = 3 for H78N, n = 9 for control and G17A. Arrowheads represent example c-Fos-positive cells. Scale bar, 100 µm. e Number of c-Fos-inducing cells in the M/T cell layer of the AOB sections from G17A-mutant-, H78N-mutant-, hemoglobin (Hb) from BALB/c-, and control buffer-stimulated male mice. n = 3 for H78N, n = 6 for BALB/c Hb, and n = 9 for control and G17A. Error bars, S.E.M. control vs. BALB/c Hb; p = 0.007, G17A vs. BALB/c Hb; p = 0.046, control vs. H78N; p = 0.058, and G17A vs. H78N; p = 0.060 by the two-sided Steel-Dwass test. f Three dimensional structure of human hemoglobin (1A3N, RCSB Protein Data Bank, https://www.rcsb.org/structure/1a3n)47. Blue and green cartoons in the model represent α-globin and β-globin, respectively. The position of the 17th glycine is highlighted by a red dot.
