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Figure 3
Purification steps and biochemical characterization of H. americanus α- and β-crustacyanins. (a) Ion-exchange chromatograms for α-crustacyanin and the loose heterodimeric β-crustacyanin subunits. (b, c) DLS analysis showing a homogenous population of monodisperse particles of α-crustacyanin. (d) Absorption spectra of purified β-crustacyanin (purple curve) and α-crustacyanin (blue curve) with maxima at 591 and 631 nm, respectively. (e) Sepharose 12 size-exclusion chromatography of α-crustacyanin with molecular-weight (MW) markers [6 × JBU (jack bean urease), MW = 544 482 kDa; 3 × SPU (Sporosarcina pasteurii urease), MW = 245 588 kDa; 2 × BSA (bovine serum albumin), MW = 132 864 kDa; BSA, MW = 66 432 kDa].

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
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