Results 131 to 140 of about 20,871 (172)

Interaction of Aliphatic Amines with Glycogen Phosphorylase

The Journal of Biochemistry, 1982
A number of aliphatic amines was shown to stimulate AMP-dependent activity of phosphorylase b. The extent of stimulation depends on the molecular structure of amines. For linear amines, the longer the linear chain, the greater the stimulation observed.
Ktenas, T. B., Oikonomakos, Nikos G., Sotiroudis, Theodore G., Nikolaropoulos, S., Evangelopoulos, A. E.   +4 more
openaire   +3 more sources

Fish muscle glycogen phosphorylase

Canadian Journal of Biochemistry, 1968
Glycogen phosphorylase b was purified 70- to 90-fold from skeletal muscle of rainbow trout (Salmo gairdneri). The purified enzyme exhibited maximal activity near pH 6.8 at 37°. Of several 5′-nucleotides tested, only 5′-AMP caused stimulation of phosphorylase b. The Km value for glucose-1-phosphate was 10–15 mM, and for 5′-AMP, 0.2–0.4 mM.
openaire   +2 more sources

Glycogen Phosphorylase b

2020
This chapter provides an account of the current understanding of the catalytic and control mechanisms of muscle glycogen phosphorylase b with special emphasis on the results from the crystal structure determination of the rabbit muscle enzyme. Glycogen phosphorylase catalyzes the first step in the intracellular degradation of glycogen.
Louise N. Johnson, Janos Hajdu, K. Ravindra Acharya, David I. Stuart, Paul J. McLaughlin, Nikos G. Oikonomakos, David Barford   +6 more
openaire   +1 more source

Glycogen synthetase and phosphorylase in developing chick glycogen body

Journal of Experimental Zoology, 1974
AbstractGlycogen synthetase and phosphorylase activities were quantitatively determined for the first time in glycogen body tissue from late embryonic and neonatal chicks. For comparative purposes, these enzyme activities were examined also in skeletal muscle and liver from pre‐ and post‐hatched chicks.
C A, Benzo, L D, De Gennaro
openaire   +2 more sources

On the activities of glycogen phosphorylase and glycogen synthase in the liver of the rat

Biochimica et Biophysica Acta (BBA) - General Subjects, 1978
A procedure was developed for determination of glycogen synthase and phosphorylase activities in liver after various in vivo physiological treatments. Liver samples were obtained from anaesthetised rats by freeze-clamping in situ. Other procedures were shown to stimulate the activity of phosphorylase and depress the activity of glycogen in the liver ...
J D, Newman, J M, Armstrong
openaire   +2 more sources

In vivo synthesis of glycogen by phosphorylase system

Histochemistry, 1980
Application of conventional histochemical techniques to the living chick retina demonstrates that phosphorylase can synthesize glycogen (polyglucose) in vivo, in the paraboloid of the accessory cone. Natural in vivo glycogen synthesis may therefore be due to glycogen synthetase and phosphorylase systems, although phosphorylase is normally regarded as a
T, Amemiya, H, Yoshida
openaire   +2 more sources

Glycogen Phosphorylase Activation by Progesterone in Liver

Experimental and Clinical Endocrinology & Diabetes, 2009
Glycogen phosphorylase activity is increased before protein synthesis activation by progesterone. This effect is not blocked by antibiotics (actinomycin D and cycloheximide) that are known to inhibit mRNA or protein synthesis. At times similar to those of phosphorylase activation, cAMP are not enhanced, as would be expected considering the classical ...
M J, Sancho, A, Gomez-Muñoz, A, Sanchez-Bueno, M, Trueba, A, Marino   +4 more
openaire   +2 more sources

Control properties of yeast glycogen phosphorylase

Biochemical and Biophysical Research Communications, 1971
Abstract Yeast glycogen phosphorylase is not AMP-sensitive and exists in enzymatically non- interconvertible forms. It is competitively inhibited in vitro by G-6-P and UDPG. Glucose also inhibits. These effectors, however, do not seem to affect the enzyme in vivo.
F, Sagardía, I, Gotay, M, Rodríguez
openaire   +2 more sources

Evolution of Allosteric Control in Glycogen Phosphorylase

Journal of Molecular Biology, 1993
In relation to the primary sequence and three-dimensional structure of rabbit muscle glycogen phosphorylase, we have carried out a comparative sequence analysis of phosphorylases from human, rat, Dictyostelium, yeast, potato and Escherichia coli. Based on sequence similarity, a large region of the protein is shared by these enzymes extending from alpha-
J W, Hudson, G B, Golding, M M, Crerar
openaire   +2 more sources

Glycogen-bound phosphorylase in Cryptococcus laurentii

Biochimica et Biophysica Acta (BBA) - General Subjects, 1970
Abstract Electron micrographs of Cryptococcus laurentii cells reveal glycogen granules throughout the cytoplasm. Glycogen phosphorylase (α-1,4-glucan: orthophosphate glucosyltransferase, EC 2.4.1.1) is bound to these granules and has been obtained in purified form upon isolation of homogeneous preparations of these granules.
J C, Schultz, H, Ankel
openaire   +2 more sources