Abstract
An assay specific for the active form of liver phosphorylase kinase (EC 2.7.1.38) has been developed utilizing inhibition of the inactive form of phosphorylase kinase by β-glycerophos, phate and ethylene glycol bis(β-aminoethyl ether) N,N′-tetraacetic acid. Following in vitro activation the results compared favorably with those obtained using a less specific assay previously available. (J. R. Vandenheede, S. Keppens, and H. DeWulf, 1977, Biochim. Biophys. Acta. 481, 463-470; D. D. Doorneweerd, A. W. H. Tan, and F. Q. Nuttall, 1978, Diabetes 27, 474). The in vitro activation of phosphorylase kinase was not associated with the formation of a small-molecular-weight form of the enzyme. The utility of the assay in monitoring in vivo interconversion reactions in response to various physiological stimuli was demonstrated.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 271-276 |
| Number of pages | 6 |
| Journal | Analytical Biochemistry |
| Volume | 113 |
| Issue number | 2 |
| DOIs | |
| State | Published - May 15 1981 |
Bibliographical note
Funding Information:This work was supported in part by grants from the American Diabetes Association of Minnesota and from Veterans Administration research funds. D. D. Door-neweerd is an Associate Investigator of the Veterans Administration. F. Q. Nuttall is a Medical Investigator of the Veterans Administration. The expert technical assistance of Ms. Maria Cremer and Ms. Diane E. Miller is gratefully acknowledged.
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
-
SDG 3 Good Health and Well-being
Fingerprint
Dive into the research topics of 'An assay specific for the active form of liver phosphorylase kinase'. Together they form a unique fingerprint.Cite this
- APA
- Standard
- Harvard
- Vancouver
- Author
- BIBTEX
- RIS