Physicochemical properties of peroxidase

Relative costs of various commercial enzymes for AA-type EIA for the preparation of monoconjugates and their relative detectabilities (all values are relative to peroxidase) 

Enzyme cat. No. Relative price/mg (a) Relative molecular weight (6) Relative conjugation efficiency (c) Relative costs able) Relative detectabilities  

Molecular composition polypeptide 308 amino acids, 33890 daltons protohematin IX and calcium 7(X) daltons carbohydrate (calculated) 9S3S daltons carbohydrate composition (residues) fucose 10, fr, 8 xylose 9, 7, 8 mannose 34, 18, 24 glucosamine 47, 17, 8 disulfide bridges 4  

Spectral optima prosthetic group ( Soret band ) 403 nm apoprotein 275 nm  

POases often occur as multiple isozymes and are widely distributed, particularly in plants (Theorell, 1942 Shannon et al., 1966). They appear to catalyze the same reaction, but differ markedly in physicochemical and kinetic properties (Shannon et al., 1966 Kay et al., 1967). It is very likely that the different iso-POases serve specialized, albeit unknown biological functions. Three main types of POases have been identified (i) the acidic (probably cell-wall-associated) POases with a very high carbohydrate content (Mazza et al., 1973 Welinder, 1979) (ii) POases with a p/around neutrality (or slightly basic) with a somewhat lower sugar content and, (iii) very basic 

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