PROPERTIES OF LOW-MOLECULAR-WEIGHT ACID-PHOSPHATASES ISOLATED FROM CYTOSOL AND CHROMATIN OF RAT-LIVER
- 1 January 1980
- journal article
- research article
- Vol. 27 (3-4) , 281-293
Abstract
Acid phosphatases (orthophosphoric-monoester phosphohydrolases, acid optimum, EC 3.1.3.2) of low MW were isolated from cytosol and chromatin of rat liver cells. The cytosolic enzyme was homogeneous on SDS[sodium dodecylsulfate]-polyacrylamide-gel electrophoresis at pH 8.3 (MW 16,000 .+-. 3000). Both enzymes showed similar electrophoretic mobility and MW but they differed in substrate specificity, response to inhibitors and susceptibility to SH-protecting reagents.This publication has 6 references indexed in Scilit:
- Lysosomal acid pyrophosphatase and acid phosphataseArchives of Biochemistry and Biophysics, 1968
- Nuclei from Rat Liver: Isolation Method That Combines Purity with High YieldScience, 1966
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- STUDIES OF ACID PHOSPHATASE. I. ELECTROPHORETIC SEPARATION OF ACID PHOSPHATASES OF RAT LIVER ON POLYACRYLAMIDE GELSJournal of Histochemistry & Cytochemistry, 1961
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951
- Possible Significance of Hexosephosphoric Esters in OssificationBiochemical Journal, 1926