Biochemical aspects of biosensors.

A review of the major types of biological molecules and systems (including antibodies, enzymes and whole cells) on which biosensors can be based is presented. Specific emphasis is placed on a critical assessment of the relative strengths and weaknesses of the respective technologies and on analysis of the importance of practical considerations such as sample interference, signal-to-noise ratio and biomolecule stability. The importance of efficient coupling of the biological and transducer components of a biosensor is highlighted. Future trends and directions in biosensor research and commercial aspects of the technology are also discussed. The article concludes with a summary of current biosensor research activities at the GEC-Marconi Hirst Research Centre.

Kinetics of heme octapeptide (microperoxidase-8; MP-8) formation studied by high-pressure liquid chromatography (HPLC) monitoring of the peptic and tryptic hydrolysis of horse heart cytochrome-c.

The kinetics of the sequential peptic and tryptic hydrolysis of cytochrome-c to give the heme-peptides microperoxidase-11 (MP-11) and -8 (MP-8), respectively, has been investigated by high performance liquid chromatography (HPLC), and we demonstrate that MP-8 can be prepared from cytochrome-c to the point of lyophilization within 4 hr.

Oxygen activation and ligand binding by pure heme-octapeptide microperoxidase-8 (MP-8).

The rapid, efficient preparation of pure microperoxidase-8 (MP-8) is described. Ligand binding studies confirm that MP-8 is monomeric in alkaline solution. It is shown that the monomeric MP-8 activates oxygen in a similar manner to that already reported for alkaline hemin, establishing the octapeptide as a possible second generation model for the oxygen activation/insertion reactions of the cytochrome P-450.