Study on the Absorption and Protein Binding 0f Carbaryl, Dieldrin and Paraquat in Rats Fed on Protein Diet
نویسندگان
چکیده
・・・・・Carbaryl was well absorbed from the small intestine of rats. In the cytosol fraction of intestinal mucosa, it was bound to a smallmolecular component (M. W. 2,200 daltons). In serum, carbaryl was bound mainly to albumin and partly te globulins. Dieldrin was slowly absorbed from small intestine. The peak of dieldrin concentration in blood was observed 2.5 hr after the administration. Binding of dieldrin te mueosal protein in cytosol was not deteetable. In serum, dieldrin was bound to lipoproteins, globulins and partly to albumin. Absorption ef paraquat from the small intestine was more rapid than that of dieldrin in situ study. Heweyer, in vivo study, the absorption of paraquat was the leWest among these three chemicals. In the cytosol fractien of intestinal mucosa, paraquat was bound to a small-molecular component (M. W. 3,100 daltons). In serum, it was present in unbound fraction. In the eomparative studies with pretein diets, absorption of paraquat from small intestine in situ was higher in low prQtein diet rats than that i" high protein diet rats. Howeyer, difference in absorption in yitro and in histopathological study wus not nQted between low pretein diet rats and high protein diet rats.
منابع مشابه
Study on the absorption and protein binding of carbaryl, dieldrin and paraquat in rats fed on protein diet.
Carbaryl was well absorbed from the small intestine of rats. In the cytosol fraction of intestinal mucosa, it was bound to a smallmolecular component (M. W. 2,200 daltons). In serum, carbaryl was bound mainly to albumin and partly to globulins. Dieldrin was slowly absorbed from small intestine. The peak of dieldrin concentration in blood was observed 2.5 hr after the administration. Binding of ...
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