Effect of mercurial compounds on structure-linked latency of lysosomal hydrolases
- 1 November 1967
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 105 (2), 685-690
- https://doi.org/10.1042/bj1050685
Abstract
1. A partially purified lysosomal preparation was obtained from adult mouse livers by sucrose-density-gradient centrifugation of a large-granule fraction. 2. This lysosome-enriched subfraction was contaminated approx. 10% by mitochondrial cytochrome c oxidase and malate dehydrogenase. 3. Free acid phosphohydrolase and β-glucuronidase contributed less than 10% of the total (Triton X-100-solubilized) activity in contrast with approx. 30% free N-acetyl-β-d-glucosaminidase when assayed in an iso-osmotic incubation system. 4. Exposure of the lysosomal preparation to inorganic Hg2+ ions and organic mercurials (p-chloromercuribenzoate, phenylmercuric acetate) induced an irreversible loss of structure-linked latency with resulting enzyme activation. 5. Maximal activation was related to log [Hg2+] and pH. The response was all-or-none for individual particles; the dose–response curve portrayed the variation in particle resistance within the lysosomal population. 6. l-Cysteine and GSH totally prevented Hg2+ ion-induced hydrolase activation. Ascorbate provided approx. 50% protection. 7. The three lysosomal hydrolases were differentially activated at constant [Hg2+], suggesting a different pattern of binding, unique for each enzyme studied.This publication has 33 references indexed in Scilit:
- Fluorometric determination of N-acetyl-β-d-glucosaminidase activityArchives of Biochemistry and Biophysics, 1967
- Studies on bone enzymes. The activation and release of latent acid hydrolases and catalase in bone-tissue homogenatesBiochemical Journal, 1965
- RAT-KIDNEY LYSOSOMES: ISOLATION AND PROPERTIESBiochemical Journal, 1965
- A note on acid phosphatase release from spleen, liver and thymus of ratsBiochimica et Biophysica Acta (BBA) - General Subjects, 1964
- Spectrofluorometric determination of β-glucuronidase activityArchives of Biochemistry and Biophysics, 1964
- Water Uptake and Extrusion by Mitochondria in Relation to Oxidative PhosphorylationPhysiological Reviews, 1962
- The hydrolysis of phenyl phosphate by mouse-liver acid phosphataseBiochemical Journal, 1961
- Tissue fractionation studies. 7. Release of bound hydrolases by means of triton X-100Biochemical Journal, 1956
- Reproducibility of Differential Centrifugation Experiments in Tissue FractionationNature, 1953
- A MICROSPECTROPHOTOMETRIC METHOD FOR THE DETERMINATION OF CYTOCHROME OXIDASEJournal of Biological Chemistry, 1951