Results 181 to 190 of about 28,187 (220)
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Molecular and Cellular Biochemistry, 1982
The presence of two interconvertible forms of phosphorylase kinase has been confirmed in rat liver extracts. The pH optimum of the nonactivated form (PhK b) was lower than the pH optimum of the activated form (PhK a) as reported by others (2). In the absence of calcium the Km of PhK b for phosphorylase b was 53 +/- 10 U/ml with a Vm of 17 +/- 1 U/gm of
D D, Doorneweerd, A W, Tan, F Q, Nuttall
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The presence of two interconvertible forms of phosphorylase kinase has been confirmed in rat liver extracts. The pH optimum of the nonactivated form (PhK b) was lower than the pH optimum of the activated form (PhK a) as reported by others (2). In the absence of calcium the Km of PhK b for phosphorylase b was 53 +/- 10 U/ml with a Vm of 17 +/- 1 U/gm of
D D, Doorneweerd, A W, Tan, F Q, Nuttall
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The phosphorylase kinase reaction on a peptide derived from glycogen phosphorylase
Biochemical and Biophysical Research Communications, 1973Abstract The phosphorylation of the peptide, Ser Asp Gln Glu Lys Arg Lys Gln-Ile Ser Val Arg Gly Leu, at the seryl residue between isoleucine and valine by phosphorylase kinase is described. No phosphorylation occurs at the seryl residue at the amino terminus.
G, Tessmer, D J, Graves
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Phosphorylase kinase from human polymorphonuclear leukocytes
Biochimica et Biophysica Acta (BBA) - Enzymology, 1979Phosphorylase kinase from human polymorphonuclear leukocytes was investigated in a gel filtered crude preparation (17,000 x g supernatant). It was found to exist in two forms, one (the phosphorylated form) more active than the other (the dephosphorylated form).
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Mycoplasma pneumoniae HPr kinase/phosphorylase.
European journal of biochemistry, 2004HPr kinase/phosphorylase (HPrK/P) is the key regulator of carbon metabolism in many Gram-positive bacteria. It phosphorylates/dephosphorylates the HPr protein of the bacterial phosphotransferase system on a regulatory serine residue in response to the nutrient status of the cell.
Matthias, Merzbacher +3 more
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[Phosphorylase kinase: mathematic modeling].
Biofizika, 2000A mathematical model of the dynamic behavior of phosphorylase kinase was devised. Based on the results obtained, the function of this protein is discussed. It is suggested that phosphorylase kinase doses in a cAMP-dependent manner additional portions of glucoso-l-phosphate, which the muscle cell receives in response to contraction.
D A, Davydov, K V, Platov, N V, Kotov
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Ca2+-dependent activation of phosphorylase by phosphorylase kinase in adipose tissue
Biochimica et Biophysica Acta (BBA) - Enzymology, 1976Phosphorylase kinase (EC 2.7.1.38) activity in crude cytosol preparations of chicken adipose tissue was assayed using as substrate either the endogenous phosphorylase b in the preparation or added purified rabbit skeletal muscle phosphorylase b. The results obtained with the two substrates were similar.
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Phosphorylase kinase: Mathematical model
2000A mathematical model of the dynamic behavior of phosphorylase kinase was devised. Based on the results obtained, the function of this protein is discussed. It is suggested that phosphorylase kinase doses in a cAMP-dependent manner additional portions of glucoso-1-phosphate, which the muscle cell receives in response to contraction.
Davydov D., Platov K., Kotov N.
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Regulation of Liver Phosphorylase Kinase
1981The structure, physical and kinetic properties as well as the regulatory mechanisms of skeletal muscle phosphorylase kinase have been studied extensively. In contrast to our current understanding of muscle phosphorylase kinase, the structure and regulatory properties of liver enzyme have not yet been fully clarified.
N. B. Livanova +3 more
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Phosphorylase Kinase in Human Muscle
The Journal of Biochemistry, 1967K, Hanabusa, H, Kobayashi
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