Effect of cations on structure-linked sedimentability of lysosomal hydrolases
- 1 August 1968
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 109 (1) , 149-154
- https://doi.org/10.1042/bj1090149
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- STRUCTURE‐LINKED ACTIVITY OF LYSOSOMAL ENZYMES IN THE DEVELOPING MOUSE BRAINJournal of Neurochemistry, 1968
- Effect of mercurial compounds on structure-linked latency of lysosomal hydrolasesBiochemical Journal, 1967
- Fluorometric determination of N-acetyl-β-d-glucosaminidase activityArchives of Biochemistry and Biophysics, 1967
- Dual Localization of β-Glucuronidase in Endoplasmic Reticulum and in LysosomesNature, 1967
- MECHANISM OF THE CATION EFFECT IN SUBFRACTIONATION OF MICROSOMESThe Journal of cell biology, 1966
- Effects of various anions and cations on the release of four dehydrogenases from brain mitochondria by a non-ionic detergentBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
- The influence of age on the activities of some acid hydrolases in the rat liver and kidneyBiochemical Journal, 1962
- Tissue fractionation studies. 3. Further observations on the binding of acid phosphatase by rat-liver particlesBiochemical Journal, 1955
- Tissue fractionation studies. 4. Comparative study of the binding of acid phosphatase, β-glucuronidase and cathepsin by rat-liver particlesBiochemical Journal, 1955
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951