Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2522740 | Biochemical Pharmacology | 2017 | 14 Pages |
Abstract
A lysosomal fraction (P-2), with 6- to 7-fold increase in acid phosphatase and a 2-fold decrease in β-glucuronidase content has been isolated and partially purified from rat liver homogenates. This fraction showed an excessive loss of β-glucuronidase but not acid phosphatase in the presence of ATP, which stabilized crude mitochondriallysosomal fractions. The anti-inflammatory agents, hydrocortisone (10â4 M), chloroquine (10â4 M) and phenylbutazone (10â4 M) showed no lysosomal membrane stabilizing activity when tested at pH 7.4 and pH 5.0. Instead, hydrocortisone and chloroquine enhanced the rate of release of acid phosphatase whereas the latter drug also enhanced the release of β-glucuronidase.
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Authors
J.O. Malbica, L.G. Hart,