HutB, the periplasmic hemin binding protein of Photobacterium damselae subsp. piscicida, was produced as a recombinant protein. UV-Vis spectrophotometrical analysis showed absorption spectral changes in hemin upon mixing it with the recombinant protein, indicating complex formation. Spectrophotometric titration of HutB with hemin showed saturation at a heme/HutB ratio of 1:1 and a binding affinity (K4) of 10μM.
Expression, purification, and characterization of the recombinant putative periplasmic hemin-binding protein (hutb) of photobacterium damselae subsp. piscicida / Andreoni, F.; Boiani, R.; Serafini, G.; Bianconi, I.; Dominici, S.; Gorini, F.; Magnani, M.. - In: BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY. - ISSN 0916-8451. - ELETTRONICO. - 73:5(2009), pp. 1180-1183. [10.1271/bbb.80732]
Expression, purification, and characterization of the recombinant putative periplasmic hemin-binding protein (hutb) of photobacterium damselae subsp. piscicida
Bianconi I.;
2009-01-01
Abstract
HutB, the periplasmic hemin binding protein of Photobacterium damselae subsp. piscicida, was produced as a recombinant protein. UV-Vis spectrophotometrical analysis showed absorption spectral changes in hemin upon mixing it with the recombinant protein, indicating complex formation. Spectrophotometric titration of HutB with hemin showed saturation at a heme/HutB ratio of 1:1 and a binding affinity (K4) of 10μM.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione
