TY - JOUR
T1 - Different forms of rat β-glucuronidase with rapid and slow clearance following intravenous injection
T2 - Selective serum enhancement of slow clearance forms by organophosphate compounds
AU - Stahl, Philip
AU - Mandell, Brian
AU - Rodman, Jane Somsel
AU - Schlesinger, Paul
AU - Lang, Stanley
PY - 1975
Y1 - 1975
N2 - Paraoxon and diisopropylfluorophosphate elicit a massive, selective increase in serum β-glucuronidase but not other lysosomal enzymes. The response is not blocked by atropine nor mimicked by neostigmine or carbachol. It is therefore not cholinergically mediated. Removal of the liver, by evisceration, abolishes the response suggesting a role for liver in mediating the organophosphate effect. β-Glucuronidase isolated by affinity chromatography from sera of organophosphate treated rats is catalytically similar to rat liver β-glucuronidase while having a lower isoelectric point. Following intravenous injection, purified rat liver microsomal and lysosomal β-glucuronidase are rapidly cleared from the circulation (t 1 2 = 7 min). In contrast, β-glucuronidase isolated from sera of organophosphate treated rats has a much slower clearance (t 1 2 = 47 min). Removal of the liver, by evisceration, severely reduces the clearance of all the enzyme preparations. Competition experiments with asialofetuin and asialoorosomucoid suggest that liver receptors for asialoglycoproteins do not mediate clearance of β-glucuronidase.
AB - Paraoxon and diisopropylfluorophosphate elicit a massive, selective increase in serum β-glucuronidase but not other lysosomal enzymes. The response is not blocked by atropine nor mimicked by neostigmine or carbachol. It is therefore not cholinergically mediated. Removal of the liver, by evisceration, abolishes the response suggesting a role for liver in mediating the organophosphate effect. β-Glucuronidase isolated by affinity chromatography from sera of organophosphate treated rats is catalytically similar to rat liver β-glucuronidase while having a lower isoelectric point. Following intravenous injection, purified rat liver microsomal and lysosomal β-glucuronidase are rapidly cleared from the circulation (t 1 2 = 7 min). In contrast, β-glucuronidase isolated from sera of organophosphate treated rats has a much slower clearance (t 1 2 = 47 min). Removal of the liver, by evisceration, severely reduces the clearance of all the enzyme preparations. Competition experiments with asialofetuin and asialoorosomucoid suggest that liver receptors for asialoglycoproteins do not mediate clearance of β-glucuronidase.
UR - http://www.scopus.com/inward/record.url?scp=0016726202&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(75)90149-6
DO - 10.1016/0003-9861(75)90149-6
M3 - Article
C2 - 242260
AN - SCOPUS:0016726202
VL - 170
SP - 536
EP - 546
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - C
ER -