Frangipane M E, Morton D J, Wooten J A, Pozsgay J M, Stull T L
Department of Pediatrics, Medical College of Pennsylvania, Philadelphia 19129.
FEMS Microbiol Lett. 1994 May 15;118(3):243-8. doi: 10.1111/j.1574-6968.1994.tb06835.x.
Binding of biotinylated human hemoglobin to Haemophilus influenzae was detected when organisms were grown in heme-deplete, but not heme-replete, conditions. Hemoglobin binding was completely inhibited by a 100-fold excess of unlabelled human hemoglobin or human hemoglobin complexed with human haptoglobin. Binding was only partially inhibited by rat hemoglobin, bovine hemoglobin, human globin, and bovine globin, and not at all by heme, human serum albumin, bovine serum albumin, human transferrin, or myoglobin. Hemoglobin binding was saturable at 16-20 ng of hemoglobin per 10(9) cfu. Binding of human hemoglobin was detected in serotypes a-f and serologically non-typable strains of H. influenzae, as well as Haemophilus haemolyticus but not Haemophilus parainfluenzae, Haemophilus aphrophilus, Haemophilus parahaemolyticus, or Escherichia coli.
当流感嗜血杆菌在血红素缺乏而非血红素充足的条件下生长时，可检测到生物素化人血红蛋白与该菌的结合。100倍过量的未标记人血红蛋白或与人触珠蛋白复合的人血红蛋白可完全抑制血红蛋白结合。大鼠血红蛋白、牛血红蛋白、人球蛋白和牛球蛋白只能部分抑制结合，而血红素、人血清白蛋白、牛血清白蛋白、人转铁蛋白或肌红蛋白则完全不能抑制结合。血红蛋白结合在每10⁹ cfu 16 - 20 ng血红蛋白时达到饱和。在流感嗜血杆菌a - f血清型和血清学不可分型菌株以及溶血嗜血杆菌中检测到了人血红蛋白的结合，但在副流感嗜血杆菌、嗜沫嗜血杆菌、副溶血嗜血杆菌或大肠杆菌中未检测到。
