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Paraoxonase (PON1) in Health and Disease: Basic and Clinical Aspects
. Ed(S): Costa, Professor Lucio G.; Furlong, Clement E.
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Description for Paraoxonase (PON1) in Health and Disease: Basic and Clinical Aspects
hardcover. PON1 metabolizes a number of drugs, activating some and inactivating others. This title describes the advances in understanding the role of PON1 in both cardiovascular disease and toxicology of insecticide exposure. It tells some of the information indicating an important possible role in the pharmacokinetics of drug metabolism. Editor(s): Costa, Professor Lucio G.; Furlong, Clement E. Num Pages: 216 pages, biography. BIC Classification: MMGT; PSBT; RN. Category: (P) Professional & Vocational; (UP) Postgraduate, Research & Scholarly; (UU) Undergraduate. Dimension: 235 x 155 x 14. Weight in Grams: 526.
The paraoxonase or PON family of genes resides on human chromosome 7q2t-22 in the order PONt, PON3 and PON2. PONt was one of the early genes identified as an environmentally relevant gene, in that it is important in determining an individual's sensitivity or resistance to exposure from specific organophosphorus (OP) insecticides. Paraoxonase (PONt) is an A esterase (i. e. , not inhibited by OP compounds) initially identified for its ability to catalytically hydrolyze paraoxon, the toxic metabolite (oxon form) of the insecticide parathion. Evidence accumulated in the past several years has established that this enzyme, which is present at variable ... Read more
The paraoxonase or PON family of genes resides on human chromosome 7q2t-22 in the order PONt, PON3 and PON2. PONt was one of the early genes identified as an environmentally relevant gene, in that it is important in determining an individual's sensitivity or resistance to exposure from specific organophosphorus (OP) insecticides. Paraoxonase (PONt) is an A esterase (i. e. , not inhibited by OP compounds) initially identified for its ability to catalytically hydrolyze paraoxon, the toxic metabolite (oxon form) of the insecticide parathion. Evidence accumulated in the past several years has established that this enzyme, which is present at variable ... Read more
Product Details
Format
Hardback
Publication date
2002
Publisher
Springer United States
Number of pages
216
Condition
New
Number of Pages
216
Place of Publication
New York, NY, United States
ISBN
9781402072826
SKU
V9781402072826
Shipping Time
Usually ships in 15 to 20 working days
Ref
99-15
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