S. Watanabe et al., Recombinant bovine lactoperoxidase as a tool to study the heme environmentin mammalian peroxidases, FEBS LETTER, 441(3), 1998, pp. 476-479
The cDNA encoding bovine lactoperoxidase (LPO) has been expressed in CHO ce
lls. The recombinant LPO mas secreted as an enzymatically active single cha
in molecule presenting two immunoreactive forms of 88 kDa and 82 kDa, diffe
ring by their glycosylation. rLPO exhibited the characteristic absorbance s
pectrum with a Soret peak at 413 nm, Engineering of rLPO into a myeloperoxi
dase (MPO)-like molecule was attempted by substituting Gln-376 by Met, a re
sidue known to achieve covalent binding with the heme in MPO. However, the
resulting bovine LPO mutant failed to acquire the peculiar absorbance spect
rum and the chlorinating activity of MPO, underlining the complex nature of
interactions in the heme vicinity, (C) 1998 Federation of European Biochem
ical Societies.