The impact of coastal realignment on the availability of ecosystem services: gains, losses and trade-offs from a local community perspective.

Coastal realignment is the procedure of repositioning or removing coastal defense structures to restore tidal flooding and facilitate the development of intertidal ecosystems in a previously reclaimed area from the sea. A key policy objective of coastal realignment is to increase ecosystem services provided by intertidal ecosystems and thereby contribute to human well-being. However, the social response to coastal realignment is often negative, raising the question as to what extent communities living nearby project locations recognize, value and benefit from the goods and services provided by restored intertidal ecosystems.

Isolation and characterisation of a class of carbohydrate oxidases from higher plants, with a role in active defence.

In a search for novel plant-derived antimicrobial proteins, we screened extracts from salicylic acid (SA)-treated lettuce and sunflower leaves. These extracts displayed very potent antimicrobial activity against a set of phytopathogens. Characterisation of these extracts revealed that in both extracts, proteins of approximately 60 kDa were responsible for the antimicrobial activity.

Studies on the effect of fenoprofen on the activation and oxidation of long chain and very long chain fatty acids in hepatocytes and subcellular fractions from rat liver.

We studied the effect of fenoprofen on the activation of palmitic acid (C16:0), lignoceric acid (C24:0) and cerotic acid (C26:0) in microsomal and peroxisomal fractions from rat liver. Fenoprofen was found to inhibit the formation of palmitoyl-CoA in both microsomal and peroxisomal fractions whereas the formation of lignoceroyl-CoA and cerotoyl-CoA was not inhibited at all. In freshly isolated rat hepatocytes palmitic acid beta-oxidation was progressively inhibited at increasing concentrations of fenoprofen, most probably due to its inhibitory effect on palmitoyl-CoA synthetase activity.

X-linked adrenoleukodystrophy: biochemical diagnosis and enzyme defect.

The adrenoleukodystrophies refer to three genetically distinct disorders all characterized by the accumulation of very long-chain fatty acids. In this paper we will review the biochemical aspects of these leukodystrophies with particular emphasis on the methods used to measure very long-chain fatty acid levels in plasma and their reliability. Furthermore, we will concentrate on the primary defect in the X-linked form of adrenoleukodystrophy.

Oxidation of very-long-chain fatty acids in rat brain: cerotic acid is beta-oxidized exclusively in rat brain peroxisomes.

We studied the effect of sodium 2-[5-(4-chlorophenyl)pentyl]oxirane-2-carboxylate (POCA), a potent inhibitor of mitochondrial carnitine palmitoyltransferase I, on fatty acid oxidation by rat brain cells. In cultured glial cells as well as in dissociated brain cells from adult rats palmitic acid (16:0) oxidation was inhibited by about 85% of control values when 25 microM POCA was added to the medium, whereas no inhibition of cerotic acid (26:0) oxidation was observed. Furthermore, omission of carnitine from the culture medium resulted in a 57.

A fluorimetric assay for acyl-CoA synthetase activities.

In this paper we describe a fluorimetric assay for the measurement of long-chain acyl-CoA synthetase activity in rat liver postnuclear supernatants. The method is based upon the use of acyl-CoA oxidase which catalyzes the dehydrogenation of acyl-CoA esters to yield enoyl-CoA esters and H2O2. H2O2 subsequently reacts with homovanillic acid in a horseradish peroxidase-catalyzed reaction to form a highly fluorescent dimer (see G.

Topography of very-long-chain-fatty-acid-activating activity in peroxisomes from rat liver.

We have investigated the localization of palmitoyl-CoA (hexadecanoyl-CoA) synthetase (EC 6.2.1.

Long-chain-acyl-CoA synthetase and very-long-chain-acyl-CoA synthetase activities in peroxisomes and microsomes from rat liver. An enzymological study.

We have investigated the palmitic acid (C16:0) and cerotic acid (C26:0) activating activities in rat-liver microsomes and peroxisomes. The activation of the two fatty acids showed similar dependencies on ATP and coenzyme A, reflected in about equal apparent Km values both in microsomes and peroxisomes. In microsomes and peroxisomes similar apparent Km values for palmitic acid were found (15 microM and 22.