Galactose oxidase source

There are a number of excellent sources of information on copper proteins notable among them is the three-volume series Copper Proteins and Copper Enzymes (Lontie, 1984). A review of the state of structural knowledge in 1985 (Adman, 1985) included only the small blue copper proteins. A brief review of extended X-ray absorption fine structure (EXAFS) work on some of these proteins appeared in 1987 (Hasnain and Garner, 1987). A number of new structures have been solved by X-ray diffraction, and the structures of azurin and plastocyanin have been extended to higher resolution. The new structures include two additional type I proteins (pseudoazurin and cucumber basic blue protein), the type III copper protein hemocyanin, and the multi-copper blue oxidase ascorbate oxidase. Results are now available on a copper-containing nitrite reductase and galactose oxidase. 

Glycoproteins have been located on the surface of two murine leukaemic cells, as shown by o-galactose oxidase-sodium borotridite and I-lacto-peroxidase-iodination techniques. The patterns on polyacrylamide gel electrophoresis of the solubilized glycoproteins from the two sources are indistinguishable but differ from those of the surface glycoproteins of HeLa cells. 

The large kinetic isotope effect observed in the oxidation of d-[6- H] galactose by galactose oxidase has been exploited to increase its specific activity. As the unlabelled substrate is oxidised faster, incomplete oxidation leaves the starting material enriched in labelled component. In the Bleomycin-mediated oxidative degradation of DNA, 2 -deo qr-4 -pentulose is released. A mechanistic study with 0-labeIled O2 and H2O revealed that the solvent is the source of the 4 -carbonyl oxygen atom. ... 

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