Monocyte Esterase Chemistry
نویسنده
چکیده
Organop iosphat, insecticides, such as Vapona, Naled, and Rabon, are highly potent inhibitors of an enzyme found in human monocytes. The enzyme, a specific monocyte esterase, could be inhibited by Vapona in blood samples via airborne contamination at levels easily achieved from commercial slow-release insecticide strips. Fifty percent inhibition (150)-as measured on the Hemalog D ( Technicon Corp.) -occurred at solution concentrations of 0.22, 1.5, and 2.6 x 1O_6 g/liter for Vapona, Rabon, and Naled, respectively. Parathion (a thiophosphate) and Baygon (a carbamate) were less potent, withl50valuesof 3.7 x iO and 1.4 x i g/Iiter, respectively. Dursbcin (another thiophosphate) and Carbaryl (a carbamate) showed only marginal inhibition. Eserine, malathion, nicotine and pyrethrum had no’ inhibitory effect up to 0.5 g/liter. The occurrence of this effect in vivo has not yet been shown, nor is it clear what the implications of such an effect would be. The inhibition of this enzyme by airborne contaminants, however, may interfere with the proper functioning of the Hemalog D.
منابع مشابه
Organophosphates and monocyte esterase deficiency.
AIMS To examine the possibility that monocyte esterase deficiency (MED) could be caused by exposure to organophosphates. METHODS Pseudocholinesterase, paraoxonase and arylesterase activities were measured in the serum and acetylcholinesterase activity was measured in the red cells of a group of monocyte esterase deficient subjects and compared with the enzyme activities of a control group of ...
متن کاملMonocyte esterase deficiency in malignant neoplasia.
A survey of the incidence of monocyte esterase deficiency in 4000 inpatients (including 808 with malignant neoplastic disease) and 474 normal controls was performed using an automated esterase method. A highly significant excess of patients with malignant disease and the deficiency was evident when compared with normal controls or all other patients. Within the group of patients with malignant ...
متن کاملcDNA cloning and characterization of human monocyte/macrophage serine esterase-1.
Human monocyte/macrophage serine esterase (HMSE), commonly known as acid esterase or alpha-naphthylacetate esterase, comprises a group of five enzyme variants that can be distinguished by their isoelectric points from esterase variants of the other normal human blood cell populations. A cDNA for one of the monocytic enzyme variants (HMSE1) was cloned from a U-937 lambda gt11 cDNA library by scr...
متن کاملcDNA Cloning and Characterization of Human Monocyte/Macrophage Serine Esterase-1
Human monocyte/macrophage serine esterase (HMSE), commonly known as acid esterase or anaphthylacetate esterase, comprises a group of five enzyme variants that can be distinguished by their isoelectric points from esterase variants of the other normal human blood cell populations. A cDNA for one of the monocytic enzyme variants (HMSE1) was cloned from a U-937 A g t l l cDNA library by screening ...
متن کاملcDNA Cloning and Characterization of Human Monocyte/Macrophage Serine Esterase-1
Human monocyte/macrophage serine esterase (HMSE), commonly known as acid esterase or anaphthylacetate esterase, comprises a group of five enzyme variants that can be distinguished by their isoelectric points from esterase variants of the other normal human blood cell populations. A cDNA for one of the monocytic enzyme variants (HMSE1) was cloned from a U-937 A g t l l cDNA library by screening ...
متن کاملMonocyte Nonspecific Esterase: Purification and Subunit Structure
Monocyte nonspecific esterase has been purified from cultured cells of the acute myeloid leukemia cell line. ML-l. The purified enzyme shows the characteristic properties of the monocyte neutral serine carboxyI esterase, with high sensitivity to organophosphorus inhibitors and sodium fluoride inhibitor. The enzyme is a membrane protein which in the native state exists as a monomer of a mol wt o...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره شماره
صفحات -
تاریخ انتشار 2005