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The sensitivity of different tissues for assessment of chronic low-dose environmental exposure of fish to alkylphenols (APs) was investigated. We exposed Atlantic cod (Gadus morhua) in the laboratory to tritium labelled 4-tert-butylphenol, 4n-pentylphenol, 4n-hexylphenol, and 4n-heptylphenol via seawater (8ng/l) and via contaminated feed (5μg/kg fish per day). Measurements of different fish tissues during eight days of exposure and eight subsequent days of recovery revealed that APs administered via spiked seawater were readily taken up whereas the uptake was far less efficient when APs were administered in spiked feed. AP residues were mainly located in the bile fluid whereas the concentrations in liver were very low, indicating a rapid excretion and the liver–bile axis to be the major route of elimination. The biological half-life of APs in the exposed cod was short, between 10 and 20h. Our study shows that in connection with biomonitoring of AP exposure in fish, assessment of AP metabolites in bile fluid is a more sensitive tool than detection of parent AP levels in liver or other internal tissues. [Copyright &y& Elsevier]

A mixture of sialylglycoasparagines and sialylglycopeptides was successively incubated with lysosomal extracts. at two pH values, first at pH 7.5 and then at pH 4. The ¹H-NMR analysis of the sialyloligosaccharides released during the enzymatic digestion demonstrates the sequential action of aspartylgiucosaminidase and an endo-N- acetyl-β-D-glucosaminidase which release sialyloligosaccharides identical to the reference sugars isolated from the urine of patients suffering from sialidosis. This process represents a new catabolic pathway for N-glycosyl-proteins which may account for the appearance of the oligosaccharides stored in tissues and urine of patients suffering from lysosomal diseases. [ABSTRACT FROM AUTHOR]

Characterizes an endo-N-acetyl-beta-D-glucosaminidase, active towards oligosaccharides, in rat liver. Determination of reaction product's primary structure through nuclear magnetic resonance spectroscopy; Location of enzyme in the lysomal fraction; Absence of enzyme reaction to conjugated glycans; Evidence of alternative pathways for the degradation of glycoprotein glycans inside lysosomes; Speculation of enzymic activity as oligosaccharide origin.

Submaxillary gland extracts have been fractionated to characterize the enzyme responsible for the T-kininogenase activity previously reported in this tissue [Damas, J. & Adam, A. (1985) Mol. Physiol 8, 307316] and to know whether this activity could be of physiological relevance, since no enzyme reacting in catalytic amounts has been described so far to be able to release a vasoactive peptide from T-kininogen. The purified enzyme, provisionally called endopeptidase K, has an apparent Mr of 27 000 when not reduced prior to analysis but 21 000 after reduction and an acidic pi of 4.3 ± 0.1. Antigenically, it is not related to tissue kallikrein. Upon incubation with purified T-kininogen it may induce a complete liberation of T-kinin from the precursor provided it is added in stoichiometric amounts. However, in parallel with the liberation of immunoreactive kinin, a proteolysis of T-kininogen is observed which is not restricted to the site of insertion of T-kinin as would be expected using a specific kininogenase. In agree-ment with these results, no change of the mean blood pressure was observed upon injection of endopeptidase K into the circulation of normal rats even if the amount of injected enzyme was up to ten times that required for tissue kallikrein to induce a significant fall in blood pressure. However, in spite of the large proteolysis induced by incubation with stoichiometric amounts of endopeptidase K, the total papain inhibiting capacity of T-kininogen as well as the value of the apparent inhi-bition constant, Ki, with this proteinase remained unchanged. Prote-olytic fragments which retain cysteine-proteinase-inhibiting activity may therefore be released from T-kininogen by endopeptidase K more easily than immunoreactive kinin, thus emphasizing a prominent function of proteinase inhibitor or of proteinase inhibitor precursor for this molecule. [ABSTRACT FROM AUTHOR]

Polar marine surface waters are characterized by high levels of dissolved oxygen, seasonally intense UV irradiance and high levels of dissolved organic carbon. Therefore, the Arctic sea-ice habitat is regarded as a strongly pro-oxidant environment, even though its significant ice cover protects the ice-associated (=sympagic) fauna from direct irradiation to a large extent. In order to investigate the level of resistance to oxyradical stress, we sampled the sympagic amphipod species Gammarus wilkitzkii during both winter and summer conditions, as well as exposed specimens to simulated levels of near-natural and elevated levels of UV irradiation. Results showed that this amphipod species possessed a much stronger antioxidant capacity during summer than during winter. Also, the experimental UV exposure showed a depletion in antioxidant defences, indicating a negative effect of UV exposure on the total oxyradical scavenging capacity. Another sympagic organism, Onisimus nanseni, was sampled during summer conditions. When compared to G. wilkitzkii, the species showed even higher antioxidant scavenging capacity.