Spermine is a substrate of lentil (Lens culinaris) seedling amine oxidase and the oxidation products are reversible inactivators of the enzyme. The spermine is oxidized at the terminal amino groups to a dialdehyde: 2 moles of hydrogen peroxide and 2 moles of ammonia per mole of spermine are formed. The pH optimum of the enzyme with spermine is 7.9 in Tl-HCl buffer; the K(m) value is 4.4. 10(-4) molar, similar to that found with other substrates (putrescine and spermidine).
Oxidation of spermine by an amine oxidase from lentil seedlings
PADIGLIA, ALESSANDRA;MEDDA, ROSARIA;
1991-01-01
Abstract
Spermine is a substrate of lentil (Lens culinaris) seedling amine oxidase and the oxidation products are reversible inactivators of the enzyme. The spermine is oxidized at the terminal amino groups to a dialdehyde: 2 moles of hydrogen peroxide and 2 moles of ammonia per mole of spermine are formed. The pH optimum of the enzyme with spermine is 7.9 in Tl-HCl buffer; the K(m) value is 4.4. 10(-4) molar, similar to that found with other substrates (putrescine and spermidine).
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