Development of a System for Biosynthesis, Isolation and Purification of the Holoform of Recombinant Human Neuroglobin and Its Characteristics

Abstract— An efficient system for the biosynthesis, isolation and purification of recombinant human neuroglobin has been developed optimized, which makes it possible to produce protein in quantities sufficient study its properties. According UV-visible, IR-, CD-, NMR spectroscopy data, is a structured holoform state. The data chromato-mass-spectrometric analysis made conclude that there correctly formed disulfide bond structure oxidized form protein. Using Raman surface-enhanced with laser excitation at 532 nm, was shown heme reduced forms vibrational degrees freedom typical b -type hemes, iron atom hexacoordinated. 633 found –SH-groups were present neuroglobin, while bridge formed. results obtained serve as basis detailed studies functioning neuroprotector, particular, during interaction cytochrome c , released from mitochondria violation their and/or morphology.