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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Hori, Y. et al.

Hori, Koyama, Fujisawa, Nakajima, Shimada, Hirose, Kohda, Akuzawa,

Protein binding of glufosinate and factors affecting it revealed by an equilibrium dialysis technique.

We investigated the protein binding of glufosinate ammonium (GLF) and several factors affecting this binding using human serum albumin (HSA) and human volunteer serum under various conditions. The mean ratios of the free GLF (RFr-GLF) to 4% HSA were examined in the sera of patients described elsewhere at GLF levels from 1 microg/mL to 500 microg/mL; the range was found to be only from 0.80 to 0.88. Neither the incubation temperature nor buffers containing different chloride ion concentrations had any effect on the RFr-GLF to HSA. Moreover, the addition of heparin, glycoprotein-alpha1-acid ( AAG), and sodium azide had no effect on the RFr-GLF. However, pH of the isotonic phosphate buffer and the addition of palmitic or oleic acid were seen to have an effect. In this study, the mean RFr-GLF to healthy human serum was 0.99. This high value was evidenced that GLF was rapidly excreted through the renal route.[1]

References

Protein binding of glufosinate and factors affecting it revealed by an equilibrium dialysis technique. Hori, Y., Koyama, K., Fujisawa, M., Nakajima, M., Shimada, K., Hirose, Y., Kohda, Y., Akuzawa, H. Journal of analytical toxicology. (2001) [Pubmed]

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