The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Purification and properties of rabbit liver phosphorylase phosphatase.
Open accessAbstract
A procedure for the purification of rabbit liver phosphorylase phosphatase is described. The specific activity of the preparation is 2,100 units/mg of protein, representing a 25,000-fold purification. During the initial steps of the purification a large activation of enzyme activity was observed. The molecular weight of the purified enzyme was estimated by Sephadex G-75 chromatography to be 35,000, and by sucrose density ultracentrifugation to be 34,000 (2.9 S). On Na dodecyl-SO4 polyacrylamide disc gel electrophoresis a single component with a molecular weight of 34,000 was observed. The pH optimum is 6.9 to 7.4, and the Km for rabbit muscle phosphorylase alpha is 2 muM. The same procedure is also applicable to the extensive purification of phosphorylase phosphatase from rabbit muscle.
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Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 317,331
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 20,298
A Method for Determining the Sedimentation Behavior of Enzymes: Application to Protein Mixtures
Martin, R. G., & Ames, B. N. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)64180-8 · Cited by 5,565
Protein Purification by Affinity Chromatography
Cuatrecasas, P. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63022-4 · Cited by 2,796
The phosphorylase b to a converting enzyme of rabbit skeletal muscle
Krebs, E. G., & Fischer, E. H. (1956) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(56)90273-6 · Cited by 484
Fischer, E. H., & Krebs, E. G. (1962) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(62)05243-x · Cited by 264
CRYSTALLINE MUSCLE PHOSPHORYLASE
Cori, G. T., & Green, A. A. (1943) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)72111-x · Cited by 245
THE RELATIONSHIP OF EPINEPHRINE AND GLUCAGON TO LIVER PHOSPHORYLASE
Wosilait, W. D., & Sutherland, E. W. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65910-1 · Cited by 229
Phosphorylase and the Control of Glycogen Degradation
(1971) · Current Topics in Cellular Regulation · doi:10.1016/b978-0-12-152804-1.50012-x · Cited by 201
Glycogen Synthetase-D Phosphatase
Kato, K., & Bishop, J. S. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44643-7 · Cited by 200
Cited by
Ramachandran, C., Goris, J., Waelkens, E., Merlevede, W., & Walsh, D. A. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61493-0 · Cited by 81
Metadata
- Authors
- Brandt, H., Capulong, Z., & Lee, E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1975-10
- Volume
- 250
- Issue
- 20
- Pages
- 8038-8044
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1591116477
- Cited by
- 273
- References
- 20
- FWCI
- 23.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
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