Results 251 to 260 of about 38,432 (313)

Coordinated shifts in gene expression and regulation during mole-rat evolution

Daunesse M, Liorzou E, Parey E, Villar D, Berthelot C.   +4 more
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From Phosphorylase to Phosphorylase Kinase

Advances in second messenger and phosphoprotein research, 1997
Glycogen phosphorylase was the first protein shown to be controlled by reversible phosphorylation (Fischer and Krebs 1955). Control by protein phosphorylation is now known to be a ubiquitous process for intracellular signalling mechanisms. There is a growing number of protein kinase and protein phosphatase structures solved by X-ray diffraction methods
L N, Johnson, D, Barford, D J, Owen, M E, Noble, E F, Garman   +4 more
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The comparative analysis of the properties and structures of purine nucleoside phosphorylases from thermophilic bacterium Thermus thermophilus HB27

Journal of Biomolecular Structure and Dynamics, 2020
Two recombinant purine nucleoside phosphorylases from thermophilic bacterium Thermus thermophilus HB27 encoded by genes TT_C1070 (TthPNPI) and TT_C0194 (TthPNPII) were purified and characterized.
V. Timofeev, I. Fateev, M. Kostromina, Y. A. Abramchik, I. Konstantinova, V. Volkov, D. Lykoshin, O. Mikheeva, T. Muravieva, R. Esipov, I. Kuranova   +10 more
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Artificial Glycosyl Phosphorylases

Chemistry – A European Journal, 2005
Abstractα‐ and β‐Cyclodextrin 6A,6D‐diacids (1 and 2), β‐cyclodextrin‐6‐monoacid (14), β‐cyclodextrin 6A,6D‐di‐O‐sulfate (16) and β‐cyclodextrin‐6‐heptasulfate (19) were synthesised. Acids 1, 2 and 14 were made from perbenzylated α‐ or β‐cyclodextrin, by diisobutylaluminum hydride (DIBAL)‐promoted debenzylation, oxidation and deprotection.
Rousseau, C., Nordstrøm, L.U., Caballero, F.O., Christensen, B., Pedersen, T.E., Bols, M.   +5 more
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Glycogen Phosphorylase Inhibitors

Mini-Reviews in Medicinal Chemistry, 2006
Type 2 diabetes is a complex metabolic disease with hyperglycemia as its recognizable hallmark. Hepatic glucose output is elevated in Type 2 diabetic patients, and evidence suggests drugs which lower hepatic glucose production are effective antihyperglycemic agents.
Brad R, Henke, Steven M, Sparks
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Human platelet phosphorylase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1969
Abstract Human platelets contain phosphorylase activity similar in some respects to that of skeletal muscle. Sucrose gradient analysis of partially purified phosphorylase revealed a phosphorylase b dimer with apparent molecular weight of 177 000, S 20, w = 8.9 S; a phosphorylase a dimer with apparent molecular weight 177 000, s 20, w = 8 ...
S, Karpatkin, R M, Langer
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Brain glycogen phosphorylase

Archives of Biochemistry and Biophysics, 1964
Abstract Brain glycogen phosphorylase has been shown to exist in an inactive and an active form. The inactive enzyme shows no activity in the absence of AMP but is maximally active in the presence of this nucleotide. The inactive enzyme has been purified 100-fold by adsorption on starch, followed by elution of other protein and finally elution of the
G I, DRUMMOND, J, KEITH, M W, GILGAN
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Lymphocyte phosphorylase kinase

International Journal of Biochemistry, 1981
Abstract 1. 1. Phosphorylase kinase from pig lymphocytes has been purified 275-fold. 2. 2. The molecular weight of the purified enzyme was found to be 200,000. 3. 3. Optimum pH of the enzyme was dependent on ATP-Mg 2+ concentration. 4. 4. Maximum activity was obtained at equivalent molar concentration of ATP and Mg 2+ . 5.
F, Javier Gella, J, Beleta, E, Concustell   +2 more
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Hybrid Enzyme of Liver Phosphorylase and Phosphorylase I

The Journal of Biochemistry, 1976
A hybrid enzyme (LI) of liver phosphorylase [EC 2.4.1.1.] (L) and phosphorylase I, which is mainly located in brain, was isolated and its enzymatic and immunological properties were examined. The following results were obtained: (1) AMP stimulated the b forms of the hybrid (LIb), I(Ib), and L(Lb); (2) in the presence of AMP, SO42- stimulated Lb more ...
S, Yonezawa, S H, Hori
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Enzymic conversion of phosphorylase a to phosphorylase b

Biochimica et Biophysica Acta, 1953
Abstract Phosphorylase b, the product of the action of a muscle enzyme (PR) on crystalline rabbit muscle phosphorylase a, has one half the molecular weight of the a form. The molecular weights are 242, 000 and 495, 000 respectively.
P J, KELLER, G T, CORI
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