Inhibition by tributyltin of herring skeletal muscle lactate dehydrogenase activity

Gronczewska, Jadwiga; Biegniewska, Anna; Ziętara, Marek S.; Skorkowski, Edward F.

doi:10.1016/j.cca.2004.02.005

Cited by 4 publications

(3 citation statements)

References 12 publications

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“…As one enzyme of the intermediary metabolism, a significant reduction in LDH was found, which was consistent with the results in catfish and carp spermatozoa when they are exposed to TBT [21]. Reduced activity of LDH could be due to a direct interaction of TBT with the enzyme protein, as added albumin was able to protect LDH activity from TBT [22]. It was also surprisingly found that LDH activity recovered to the control level when exposed to 25 mg L -1 TBT.…”

Section: Discussionsupporting

confidence: 76%

A microcalorimetric assay of tetrahymena thermophila for assessing tributyltin acute toxicity

Chen

Feng

et al. 2008

J Therm Anal Calorim

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The power-time curves of Tetrahymena thermophila exposed to tributyltin (TBT) were detected by microcalorimetry. Metabolic rate (r) decreased significantly while peak time (PT) increased with the enhancement of TBT level. Compared with the measured multibiomarker including catalase, lactate dehydrogenase, glutathione S-transferase, ATPase and membrane fluidity, PT and r could be sensitive biomarkers for assessing TBT toxicity at cellular level. The effective concentrations obtained by them were consistent to those obtained by the protozoan community toxicity test. As a result, the microcalorimetric assay of T. thermophila had a great potential in assessing TBT acute toxicity and monitoring TBT pollution in the freshwater ecosystem.

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Section: Discussionsupporting

confidence: 76%

A microcalorimetric assay of tetrahymena thermophila for assessing tributyltin acute toxicity

Chen

Feng

et al. 2008

J Therm Anal Calorim

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“…Although it is clear that the immune system is a target for TBT toxicity [34,49], our TBT exposure shows that there is no significant impact on the expression of saMpeg1. Most of the available information concerning the immunotoxicity of TBT to mollusks, mainly inhibition of phagocytosis, has been obtained from Mytilus edulis [50], Tapes philippinarum [51] and Mya arenaria [52].…”

Section: Discussionmentioning

confidence: 98%

Molecular cloning and responsive expression of macrophage expressed gene from small abalone Haliotis diversicolor supertexta

Wang

Zhang

et al. 2008

Fish & Shellfish Immunology

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“…Based on the supplier’s specification, the antibodies contain 1–5% BSA as a protection additive. There are reported bioactivity protection methods in the literature, but most of these methods focus on the protection of the activity and stability of proteins and enzymes from the inhibition induced by temperature, soluble additives, and even radiation. − In those methods, BSA is a widely used stabilizer that prevents the thermally induced inactivation of biomolecules. Moreover, BSA has also been reported to have a protection effect on enzyme activity from the inhibition caused by a toxicant.…”

Section: Introductionmentioning

confidence: 99%

Strategy To Enhance the Wettability of Bioacive Paper-Based Sensors

Tian

Jarujamrus

et al. 2012

ACS Appl. Mater. Interfaces

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This paper reports a potential method that can restore the wettability of bioactive paper-based sensors while maintaining their bioactivity. This study is driven by the need to increase the wettability of the antibody-loaded blood typing paper devices in order to increase the blood typing assaying speed using such paper devices. Plasma treatment is used to improve the wettability of bioactive paper; the protective effect of bovine serum albumin (BSA) to biomolecules against plasma deactivation is investigated. In the first stage, horseradish peroxidase (HRP) was used as a model biomolecule, because of the convenience of its quantifiable colorimetric reaction with a substrate. By using this protection approach, the inactivation of biomolecules on paper during the plasma treatment is significantly slowed down. This approach enables plasma treatment to be used for fabricating paper-based bioactive sensors to achieve strong wettability for rapid penetration of liquid samples or reagents. Finally, we demonstrate the use of plasma treatment to increase the wettability of antibody treated blood typing paper. After the treatment, the blood typing paper becomes highly wettable; it allows much faster penetration of blood samples into the plasma treated testing paper. Antibodies on the paper are still sufficiently active for blood typing and can report patients' blood type accurately.

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Inhibition by tributyltin of herring skeletal muscle lactate dehydrogenase activity

Cited by 4 publications

References 12 publications

A microcalorimetric assay of tetrahymena thermophila for assessing tributyltin acute toxicity

A microcalorimetric assay of tetrahymena thermophila for assessing tributyltin acute toxicity

Molecular cloning and responsive expression of macrophage expressed gene from small abalone Haliotis diversicolor supertexta

Strategy To Enhance the Wettability of Bioacive Paper-Based Sensors

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