ABSTRACT
Tuna-farming is expanding worldwide, necessitating the monitoring/managing of its effects on the natural environment. In Japan, tuna-farming is conducted on coral reefs that have been damaged by mass-bleaching events and crown-of-thorns starfish (COTS) outbreaks. This study focused on the coral community on an artificial substrate of tuna-farm to reveal the possible effects of tuna-farming on the natural environment. Corals flourished on ropes suspended in the farm in the Amami Islands, southern Japan. These were moored 3 m below the sea-surface in 50-m-deep water. The coral community on the rope was analyzed and compared with those on natural substrata on two adjacent COTS-damaged reefs and with that in a protected reef. Corals were monitored throughout a year. Sixty coral species grew on the ropes, that corresponds to 27.3% of the 220 species known from Amami. The coral community was unique, dominated by massive faviid corals. On the ropes, the water temperature rarely exceeded 30.0 °C and no corals on the rope were severely bleached or covered by sedimentation during the observations. The tuna-farm infrastructure provided corals with a suitable habitat, and species-rich coral communities were established. These coral communities are an important node connecting tuna-farms and the natural environment.
Subject(s)
Anthozoa , Biodiversity , Fisheries , Animals , Anthozoa/classification , Coral Reefs , Japan , Population Dynamics , TunaABSTRACT
We examined the influence of oxidative stress on the relative amounts of various albumin-bound thiols in human plasma. To determine the ratio of thiols existing as mixed disulfides following oxidation, we developed a method combining fast purification of albumin using affinity columns and high-performance liquid chromatography (HPLC) with fluorescence detection for low molecular weight thiols which were labeled after reduction. When the effect of exposure of plasma to radical oxygen species on binding of thiols to albumin was determined by the present method, significant increases in the ratio of cysteine bound to albumin (Alb-Cys) to total cysteine were clearly demonstrated.
Subject(s)
Biomarkers/analysis , Chromatography, Affinity/methods , Chromatography, High Pressure Liquid/methods , Cysteine/metabolism , Serum Albumin/chemistry , Sulfhydryl Compounds/blood , Adult , Fluorescence , Humans , Middle Aged , Oxidative Stress/physiology , Reproducibility of Results , tert-Butylhydroperoxide/pharmacologyABSTRACT
We developed a non-radioactive and sensitive assay method for measurement of the HTL hydrolase (HTLase) activity in biological samples, using OPA as a fluorescent post-labeling agent, l-homocysteine thiolactone (L-HTL) as the substrate, and HPLC to achieve rapid and selective separation of the substrate and product. The method was applied to measure the activity of HTLase in human, rabbit, rat and mouse serum samples. In addition, the correlation between the serum HTLase activity and PON1 polymorphisms in Japanese subjects was also investigated. The serum HTLase activity in humans, as determined by measurement of the enzyme activity in 22 subjects, was found to be in the range of 0.89-2.06 nmol/min mg protein, with a mean activity of 1.44 nmol/min mg protein.
Subject(s)
Aryldialkylphosphatase/blood , Chromatography, High Pressure Liquid/methods , Adult , Animals , Aryldialkylphosphatase/genetics , Aryldialkylphosphatase/isolation & purification , Female , Genotype , Humans , Japan , Male , Mice , Middle Aged , Polymorphism, Genetic , Rabbits , Rats , Reference Values , Sensitivity and Specificity , Spectrometry, FluorescenceABSTRACT
A sensitive and simple method utilising fluorometric detection for the simultaneous routine monitoring of homocysteine thiolactone (HTL) and homocysteine (Hcy) in biological samples has been developed. Separation relies on isocratic ion-pairing and reversed-phase chromatography while the principle of the detection is that the lactone ring in HTL molecule is cleaved with an alkali to produce Hcy, which reacts with ortho-phthalaldehyde (OPA) in the absence of an added thiol reagent to form a stable fluorescent derivative. The method has a sensitivity of 200 fmol of HTL and 100 fmol for Hcy in the sample. The present method was applied to the determination of HTL and Hcy in Hep G2 cell.
