Characterization of recombinant human endothelial nitric-oxide synthase purified from the yeast Pichia pastoris.
Leber A, Hemmens B, Klösch B, Goessler W, Raber G, Mayer B, Schmidt K.
Leber A, et al. Among authors: mayer b.
J Biol Chem. 1999 Dec 31;274(53):37658-64. doi: 10.1074/jbc.274.53.37658.
J Biol Chem. 1999.
PMID: 10608822
Free article.
Upon low temperature gel electrophoresis the untreated protein appeared mainly as a monomer (88 +/- 3%), but pretreatment with H(4)biopterin and L-arginine led to a pronounced shift toward dimers (77 +/- 4%). Thus, in contrast to bovine eNOS (List, B. M., Klosch, B. …
Upon low temperature gel electrophoresis the untreated protein appeared mainly as a monomer (88 +/- 3%), but pretreatment with H(4)biopterin …