Half-copper-depleted and fully copper-depleted amine oxidase from bovine serum were reconstituted with either copper or cobalt. All samples were studied by high-sensitivity scanning calorimetry, by enzyme activity analysis, and by reactivity with phenylhydrazine. The calorimetric profile of the protein was strongly modified by the removal of a single Cu ion approximately to the same extent as by complete copper removal, in agreement with the loss of over 80% enzymic activity. The thermograms of metal-reconstituted species showed a marked similarity with that of the native enzyme, irrespective of whether copper or cobalt was present. Reactivity with phenylhydrazine and enzymic activity measurements showed that in cobalt-substituted amine oxidase the organic cofactor was reactive and the enzyme was catalytically competent, although kinetically less efficient. These observations agree both with previous findings on the protein half-site reactivity and with previous suggestions for a copper conformational role in bovine serum amine oxidase, namely of maintaining a functional conformation at the active site.
PROPERTIES OF COBALT-SUBSTITUTED BOVINE SERUM AMINE OXIDASE / Agostinelli, Enzo; Laura, Morpurgo; Changqing, Wang; Giartosio, Anna; Bruno, Mondovi. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - 222:3(1994), pp. 727-732. [10.1111/j.1432-1033.1994.tb18918.x]
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|Titolo:||PROPERTIES OF COBALT-SUBSTITUTED BOVINE SERUM AMINE OXIDASE|
|Data di pubblicazione:||1994|
|Citazione:||PROPERTIES OF COBALT-SUBSTITUTED BOVINE SERUM AMINE OXIDASE / Agostinelli, Enzo; Laura, Morpurgo; Changqing, Wang; Giartosio, Anna; Bruno, Mondovi. - In: EUROPEAN JOURNAL OF BIOCHEMISTRY. - ISSN 0014-2956. - 222:3(1994), pp. 727-732. [10.1111/j.1432-1033.1994.tb18918.x]|
|Appartiene alla tipologia:||01a Articolo in rivista|