Immobilization of proteins on a surface plasmon resonance (SPR) transducer is a delicate procedure since loss of protein bioactivity can occur upon contact with the untreated metal surface. Solution to the problem is the use of an immobilization matrix having a complex structure. In this paper we study the impact of direct immobilization of heme proteins (hemoglobin (Hb) and myoglobin (Mb)) on their bioactivity. We have used spin coating, for direct immobilization and matrix-assisted pulsed-laser evaporation (MAPLE)  for elaboration of the SPR biochip. The performance of both SPR chips – direct and MAPLE immobilized, was studied by SPR registration of the binding activity of Hb and Mb ligands with carbon monoxide (CO), carbon dioxide (CO2) and nitride oxide (NO). The experimental facts showed that direct immobilization of an intact molecule was achieved
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