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) |
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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.