1,4,alpha-glucan 6-alpha-glucosyltransferase deficiency|Amylopectinosis|Andersen disease|Andersens disease|Brancher deficiency glycogen storage disease|Branching enzyme deficiency|Branching-transferase deficiency glycogenosis|Cardiac glycogen phosphorylase kinase deficiency|Cardiac glycogen phosphorylase kinase deficiency (disorder)|Danon disease|Danon disease (disorder)|Deficiency of alpha-dextrin endo-1,6-alpha-glucosidase|Deficiency of alpha-dextrin endo-1,6-alpha-glucosidase (disorder)|Deficiency of alpha-galactosidase|Deficiency of alpha-galactosidase (disorder)|Deficiency of melibiase|Fanconi-Bickel syndrome|GSD IV|GSD VI|GSD VII|GSD VIII|GSD X|Glycogen phosphorylase kinase deficiency|Glycogen phosphorylase kinase deficiency (disorder)|Glycogen phosphorylase kinase deficiency, X-linked|Glycogen phosphorylase kinase deficiency, X-linked (disorder)|Glycogen phosphorylase kinase deficiency, autosomal recessive|Glycogen phosphorylase kinase deficiency, autosomal recessive (disorder)|Glycogen storage

Accepted name: phosphorylase kinase. Reaction: 2 ATP + phosphorylase b = 2 ADP + phosphorylase a. Other name(s): dephosphophosphorylase kinase; glycogen phosphorylase kinase; PHK; phosphorylase b kinase; phosphorylase B kinase; phosphorylase kinase (phosphorylating); STK17. Systematic name: ATP:phosphorylase-b phosphotransferase. Comments: Requires Ca2+ and calmodulin for activity. The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b. For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase. The enzyme couples muscle contraction with energy production via glycogenolysis glycolysis by catalysing the Ca2+-dependent phosphorylation and activation of glycogen phosphorylase b [5]. The γ subunit of the tetrameric αβγδ enzyme is the catalytic subunit.. Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 9001-88-1. References:. 1. Krebs, ...

BACKGROUND Phosphorylase kinase (PhK), also known as adenosine triphosphate (ATP)-phosphorylase b phosphotransferase, integrates multiple calcium/calmodulin-dependent signalling pathways, including those involved in cell migration and cell proliferation, while coupling these pathways to glycogenolysis and ATP-dependent phosphorylation, thus ensuring continuing energy supply for these activities. OBJECTIVES Our laboratory recently reported correlation of elevated PhK activity with psoriatic activity. This study further evaluates the significance of drug-induced suppression of PhK activity on psoriatic activity. PATIENTS AND METHODS PhK activity was assayed in four groups, each with 10 patients: (i) active untreated psoriasis; (ii) resolving psoriasis treated by calcipotriol (Dovonex(R), Bristol Myers Squibb, Princeton, NJ, U.S.A. ), a vitamin D3 analogue and an indirect inhibitor of PhK; (iii) curcumin (diferuloylmethane), a selective PhK inhibitor; and (iv) 10 normal non-psoriatic subjects.

Skeletal-muscle phosphorylase kinase is a hexadecameric oligomer composed of equivalent amounts of four different subunits, (alpha beta gamma delta)4. The delta-subunit, which is calmodulin, functions as an integral subunit of the oligomer, and the gamma-subunit is catalytic. To learn more about intersubunit contacts within the hexadecamer and about the roles of individual subunits, we induced partial dissociation of the holoenzyme with low concentrations of urea. In the absence of Ca2+ the quaternary structure of phosphorylase kinase is very sensitive to urea over a narrow concentration range. Gel-filtration chromatography in the presence of progressively increasing concentrations of urea indicates that between 1.15 M- and 1.35 M-urea the delta-subunit dissociates, allowing extensive formation of complexes larger than the native enzyme that contain equivalent amounts of alpha-, β- and gamma-subunits. As the urea concentration is increased to 2 M and 3 M, nearly all of the enzyme aggregates to ...

FTIs represent one of the first classes of antineoplastic agents designed through rational drug design. The high prevalence of activating Ras mutations in human cancers (1) initially suggested that approximately 25% of human malignancies may demonstrate sensitivity to such agents (32) . However, two critical observations have made this prediction more complex. First, the presence or absence of Ras mutations does not appear to be the sole determinant of FTI efficacy, at least in cell lines (21) . Second, H-Ras-transformed cells appear to be more sensitive to these agents than those transformed by either K-Ras or N-Ras (20 , 31 , 33 , 34) .. The first observation has cast doubts on whether Ras is a major therapeutic target of FTIs in vivo. This is because in addition to Ras, approximately 0.5% of all of the cellular proteins undergo farnesylation (19) , including nuclear laminin A and B, skeletal muscle phosphorylase kinase, and retinal proteins, as well as other members of the Ras superfamily ...

1. The properties of phosphorylase a, phosphorylase b, phosphorylase kinase and phosphorylase phosphatase present in a human haemolysate were investigated. The two forms of phosphorylase have the same affinity for glucose 1-phosphate but greatly differ in Vmax. Phosphorylase b is only partially stimulated by AMP, since, in the presence of the nucleotide, it is about tenfold less active than phosphorylase a. In a fresh human haemolysate phosphorylase is mostly in the b form; it is converted into phosphorylase a by incubation at 20degreesC, and this reaction is stimulated by glycogen and cyclic AMP. Once activated, the enzyme can be inactivated after filtration of the haemolysate on Sephadex G-25. This inactivation is stimulated by caffeine and glucose and inhibited by AMP and fluoride. The phosphorylase kinase present in the haemolysate can also be measured by the rate of activation of added muscle phosphorylase b, on addition of ATP and Mg2+. 2. The activity of phosphorylase kinase was measured ...

TY - JOUR. T1 - Phosphorylation of glycogen synthase by phosphorylase kinase. Stoichiometry, specificity and site of phosphorylation. AU - Soderling, Thomas. AU - Sheorain, Virender S.. AU - Ericsson, Lowell H.. PY - 1979/10/1. Y1 - 1979/10/1. UR - http://www.scopus.com/inward/record.url?scp=0018533336&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0018533336&partnerID=8YFLogxK. U2 - 10.1016/0014-5793(79)80723-1. DO - 10.1016/0014-5793(79)80723-1. M3 - Article. C2 - 115711. AN - SCOPUS:0018533336. VL - 106. SP - 181. EP - 184. JO - FEBS Letters. JF - FEBS Letters. SN - 0014-5793. IS - 1. ER - ...

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pep:known chromosome:VEGA66:X:102513975:102644246:-1 gene:OTTMUSG00000018059 transcript:OTTMUST00000043585 gene_biotype:protein_coding transcript_biotype:protein_coding gene_symbol:Phka1 description:phosphorylase kinase alpha 1 ...

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Comparer et commander les protéines PHKA2 pour de nombreuses espèces différentes. Trouver le bon produit sur anticorps-enligne.fr.

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PHKG1 - PHKG1 (untagged)-Kinase deficient mutant (K49M) of Human phosphorylase kinase, gamma 1 (muscle) (PHKG1) available for purchase from OriGene - Your Gene Company.

Complete information for PHKA1 gene (Protein Coding), Phosphorylase Kinase Regulatory Subunit Alpha 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

Complete information for PHKA2 gene (Protein Coding), Phosphorylase Kinase Regulatory Subunit Alpha 2, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium

The mitogen-activated protein kinase (MAPK) cascade is a highly conserved module that is involved in various cellular functions, including cell proliferation, differentiation and migration. Mammals express at least four distinctly regulated groups of MAPKs, extracellular signal-related kinases (ERK)-1/2, Jun amino-terminal kinases (JNK1/2/3), p38 proteins (p38alpha/beta/gamma/delta) and ERK5, that are activated by specific MAPKKs: MEK1/2 for ERK1/2, MKK3/6 for the p38, MKK4/7 (JNKK1/2) for the JNKs, and MEK5 for ERK5. Each MAPKK, however, can be activated by more than one MAPKKK, increasing the complexity and diversity of MAPK signalling. Presumably each MAPKKK confers responsiveness to distinct stimuli. For example, activation of ERK1/2 by growth factors depends on the MAPKKK c-Raf, but other MAPKKKs may activate ERK1/2 in response to pro-inflammatory stimuli ...

The mitogen-activated protein kinase (MAPK) cascade is a highly conserved module that is involved in various cellular functions, including cell proliferation, differentiation and migration. Mammals express at least four distinctly regulated groups of MAPKs, extracellular signal-related kinases (ERK)-1/2, Jun amino-terminal kinases (JNK1/2/3), p38 proteins (p38alpha/beta/gamma/delta) and ERK5, that are activated by specific MAPKKs: MEK1/2 for ERK1/2, MKK3/6 for the p38, MKK4/7 (JNKK1/2) for the JNKs, and MEK5 for ERK5. Each MAPKK, however, can be activated by more than one MAPKKK, increasing the complexity and diversity of MAPK signalling. Presumably each MAPKKK confers responsiveness to distinct stimuli. For example, activation of ERK1/2 by growth factors depends on the MAPKKK c-Raf, but other MAPKKKs may activate ERK1/2 in response to pro-inflammatory stimuli. Source: KEGG http://www.genome.jp/dbget-bin/www_bget?pathway:map04010 ...

The mitogen-activated protein kinase (MAPK) cascade is a highly conserved module that is involved in various cellular functions, including cell proliferation, differentiation and migration. Mammals express at least four distinctly regulated groups of MAPKs, extracellular signal-related kinases (ERK)-1/2, Jun amino-terminal kinases (JNK1/2/3), p38 proteins (p38alpha/beta/gamma/delta) and ERK5, that are activated by specific MAPKKs: MEK1/2 for ERK1/2, MKK3/6 for the p38, MKK4/7 (JNKK1/2) for the JNKs, and MEK5 for ERK5. Each MAPKK, however, can be activated by more than one MAPKKK, increasing the complexity and diversity of MAPK signalling. Presumably each MAPKKK confers responsiveness to distinct stimuli. For example, activation of ERK1/2 by growth factors depends on the MAPKKK c-Raf, but other MAPKKKs may activate ERK1/2 in response to pro-inflammatory stimuli ...

The mitogen-activated protein kinase (MAPK) cascade is a highly conserved module that is involved in various cellular functions, including cell proliferation, differentiation and migration. Mammals express at least four distinctly regulated groups of MAPKs, extracellular signal-related kinases (ERK)-1/2, Jun amino-terminal kinases (JNK1/2/3), p38 proteins (p38alpha/beta/gamma/delta) and ERK5, that are activated by specific MAPKKs: MEK1/2 for ERK1/2, MKK3/6 for the p38, MKK4/7 (JNKK1/2) for the JNKs, and MEK5 for ERK5. Each MAPKK, however, can be activated by more than one MAPKKK, increasing the complexity and diversity of MAPK signalling. Presumably each MAPKKK confers responsiveness to distinct stimuli. For example, activation of ERK1/2 by growth factors depends on the MAPKKK c-Raf, but other MAPKKKs may activate ERK1/2 in response to pro-inflammatory stimuli ...

The mitogen-activated protein kinase (MAPK) cascade is a highly conserved module that is involved in various cellular functions, including cell proliferation, differentiation and migration. Mammals express at least four distinctly regulated groups of MAPKs, extracellular signal-related kinases (ERK)-1/2, Jun amino-terminal kinases (JNK1/2/3), p38 proteins (p38alpha/beta/gamma/delta) and ERK5, that are activated by specific MAPKKs: MEK1/2 for ERK1/2, MKK3/6 for the p38, MKK4/7 (JNKK1/2) for the JNKs, and MEK5 for ERK5. Each MAPKK, however, can be activated by more than one MAPKKK, increasing the complexity and diversity of MAPK signalling. Presumably each MAPKKK confers responsiveness to distinct stimuli. For example, activation of ERK1/2 by growth factors depends on the MAPKKK c-Raf, but other MAPKKKs may activate ERK1/2 in response to pro-inflammatory stimuli ...

Songyang Z, Lu KP, Kwon YT, Tsai LH, Filhol O, Cochet C, Brickey DA, Soderling TR, Bartleson C, Graves DJ, Demaggio AJ, Hoekstra MF, Blenis J, Hunter T, Cantley LC. A structural basis for substrate specificities of protein ser/thr kinases-primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, Cdk5 and ERK1. Mol Cell Biol 1996;16:6486-93 ...

The goal of research in molecular pharmacology is to understand the action of hormones and drugs on the molecular components of their target cells. Dr. Edwin G. Krebs, Emeritus Professor of Pharmacology and Biochemistry and Emeritus Investigator of the Howard Hughes Medical Institute, is a pioneer in unraveling the complex pathways by which hormones and drugs regulate cellular functions. In 1955, Dr. Krebs and Dr. Edmond Fischer, working in the Department of Biochemistry at the University of Washington, discovered the process of protein phosphorylation as the final chemical reaction in the hormonal pathway that regulates metabolism of glycogen, a complex carbohydrate used as an energy storage molecule in cells.. The enzyme that carries out this chemical reaction, phosphorylase kinase, was the first example of a protein kinase, a family of enzymes now known to be the most important regulators of cell function. In further studies of this process in 1968, Dr. Krebs and his associates discovered a ...

The effects of food deprivation on body weight, liver weight, hepatic glycogen content, glycogenolytic enzymes and blood metabolites were compared in young and old phosphorylase b kinase-deficient (gsd/gsd) rats. Although the concentration of glycogen in liver from 9-week-old female gsd/gsd rats (730 mumol of glucose equivalents/g wet wt.) was increased by 7-8% during starvation, total hepatic glycogen was decreased by 12% after 24 h without food. In 12-month-old male gsd/gsd rats the concentration of liver glycogen (585 mumol of glucose equiv./g wet wt.) was decreased by 16% and total hepatic glycogen by nearly 40% after food deprivation for 24 h. Phosphorylase b kinase and phosphorylase a were present at approx. 10% of the control activities in 9-week-old gsd/gsd rats, but both enzyme activities were increased more than 3-fold in 12-month-old affected rodents. It is concluded that the age-related ability to mobilize hepatic glycogen appears to result from the augmentation of phosphorylase b ...

X-linked liver glycogenosis (XLG), also known as glycogen storage disease (GSD) type-IXa, is characterized by hepatomegaly, abnormal liver functions and growth retardatio..

Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity).

The sequence of events set in motion through the activation of adenyl cyclase by E is: increase in cyclic 3,5-AMP → activation of phosphorylase b kinase → increase in phosphorylase a → increase in glycogen breakdown. Since cyclic 3,5-AMP is destroyed by a phosphodiesterase, its actual level in the tissues will depend on the relative rates of two opposing reactions, catalyzed by cyclase and diesterase (1, 20). Posner et al. (16) have shown that the concentration of cyclic 3,5-AMP increases in frog muscle after E administration. Concentrations of the order of 1 x 10-7 to 1 x 10-6 M activate the phosphorylase b kinase of muscle both in vivo and in vitro (10, 16). Phosphofructokinase, on the other hand, is activated in vitro by concentrations of cyclic 3,5-AMP so much higher than are present in muscle that one wonders whether this activation is of physiological importance (13). In the isolated frog sartorius incubated at 20°C in 5 x 10-7 M E a rise in phosphorylase a can be ...

Phkg1 - Phkg1 (Myc-DDK-tagged) - Mouse phosphorylase kinase gamma 1 (Phkg1) available for purchase from OriGene - Your Gene Company.

In addition, we examined the relative PhKG1 levels inside a panel of various human tumor samples, acquired like a in a commercial sense available cDNA array. Using quantitative PCR, we learned that PhKG1 mRNA levels are elevated by a lot more than two-fold in nearly all human growths examined ). Oddly MK-2206 enough, there is no upregulation of PhKG1 detected in cancer of the prostate, recommending that PhKG1 upregulation, although common, isnt a universal sign of all tumor types which cancer of the prostate might not represent a kind that will take advantage of PhKG1 focusing on. This data offers the first proof of upregulated PhKG1 mRNA expression levels in a number of human tumor types and indicates that the upregulation of PhKG1 might be connected with cancer progression.. Discussion PhKG1 hasnt formerly been suggested as a factor either in tumorigenesis or angiogenesis. We therefore provide here the very first description from the participation of PhK within the angiogenesis process and ...

Anti-glycogen phosphorylase antibodiesGlycogen phosphorylase (EC 2.4.1.1) is an enzyme which is catalyzing the rate limiting step in the degradation of glycogen in animals by releasing glucose-1-phosphate from the terminal alpha1,4-glycosidic bond.

Use Bio-Rads PrimePCR assays, controls, templates for your target gene. Every primer pair is optimized, experimentally validated, and performance guaranteed.

The 14-3-3 protein translates the NA+,K+-ATPase {alpha}1-subunit phosphorylation signal into binding and activation of phosphoinositide 3-kinase during endocyto

Enzimler E-kitap okumak için tıklayın İçindekiler Enzimlerin kimyasal yapıları Enzimlerin tesir mekanizması Aktivatörler Spesifik İon Aktivatörleri Koenzimler İnhibitörler Non kompetetif inhibitörler Kompetitif inhibitörler Diğer inhibitörler Enzimatik reaksiyonların hızı üzerine tesir eden faktörler Enzim konsantrasyonu Substrat konsantrasyonu pH hidrogen ion konsantrasyonu Isı Reaksiyon ürünleri Kofaktör konsantrasyonu ve diğer fiziksel faktörler Zaman Enzimatik […]. ...

The PHKG2 gene provides instructions for making one piece, the gamma subunit, of the phosphorylase b kinase enzyme. This enzyme is made up of 16 subunits, four each of the alpha, beta, gamma, and delta subunits. (Each subunit is produced from a different gene.) The gamma subunit performs the function of phosphorylase b kinase enzyme, and the other subunits help regulate its activity. This enzyme is found in various tissues, although it is most abundant in the liver and muscles. One version of the enzyme is found in liver cells and another in muscle cells. The gamma-2 subunit produced from the PHKG2 gene is part of the enzyme found in the liver.. Phosphorylase b kinase plays an important role in providing energy for cells. The main source of cellular energy is a simple sugar called glucose. Glucose is stored in muscle and liver cells in a form called glycogen. Glycogen can be broken down rapidly when glucose is needed, for instance to maintain normal levels of glucose in the blood between meals. ...

Phosphorylase b is a non-active form and is present in resting muscle. Phosphorylase b kinase activity increases significantly when the Mg2+:ATP ratio exceeds. The breakd

Phosphorylase B, 1 ml. Phosphorylase a is the active form of glycogen phosphorylase that is derived from the phosphorylation of the inactive form, phosphorylase b.

P48736: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform; PI3-kinase subunit gamma; PI3K-gamma; PI3Kgamma; PtdIns-3-kinase subunit gamma; 2.7.1.153; Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma; PtdIns-3-kinase subunit p110-gamma; p110gamma; Phosphoinositide-3-kinase catalytic gamma polypeptide; Serine/threonine protein kinase PIK3CG; 2.7.11.1; p120- ...

We propose that a combination of laminaribiose and β-1,3-oligoglucan phosphorylases could be used for a one-pot enzymatic synthesis of β-1,3-oligosaccharides starting from readily available starting materials, glucose and glucose-1-phosphate. Thus, enzymatic synthesis could provide an effective way of producing designer β-1,3-oligosaccharides, compounds which potentially have several biotechnological application. However, successful biotechnological application of phosphorylases is hampered by rather limited availability of these enzymes, in fact only a small number of organisms has proven to possess enzymes with β-1,3-glucan phosphorylase activity. Our goal is to uncover potential candidates capable of demonstrating such activities and test them in practical applications. In order to achieve this goal we have undertaken research which is based on several approaches:. ...

Gene List: AGL, ALDOA, ENO3, EPM2A, FBP1, G6PC, GAA, GBE1, GYG1, GYS1, GYS2, LAMP2, LDHA, NHLRC1, PFKM, PGAM2, PGK1, PGM1, PHKA1, PHKA2, PHKB, PHKG2, PRKAG2…

1ABB: Control of phosphorylase b conformation by a modified cofactor: crystallographic studies on R-state glycogen phosphorylase reconstituted with pyridoxal 5-diphosphate.

4PHK: The Structural Basis of Differential Inhibition of Human Calpain by Indole and Phenyl alpha-Mercaptoacrylic Acids. The complex with (Z)-3-(4-chlorophenyl)-2-mercaptoacrylic acid

InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.

Created after (Sernee et al., Cell Host & Microbe, 2019), in press [PMID=31513773]. The dual activity mannosyltransferases/phosphorylases of six Leishmania proteins allows the management of mannogen (storage polysacharride). Family evolutionary related the bacterial GH130 phosphorylases ...

Glycogen phosphorylase is regulated by both allosteric control and by phosphorylation.. Hormones such as epinephrine, insulin and glucagon regulate glycogen phosphorylase using second messenger amplification systems that are linked to G proteins. Glucagon activates adenylate cyclase through a seven transmembrane receptor coupled to Gs which, in turn, activates adenylate cyclase to increase intracellular concentrations of cAMP. cAMP binds to and releases an active form of protein kinase A (PKA). Next, PKA phosphorylates phosphorylase kinase, which, in turn, phosphorylates glycogen phosphorylase b, transforming it into the active glycogen phosphorylase a. This phosphorylation is added onto the glycogen phosphorylase b serine 14. In the liver, glucagon activates another G-protein-linked receptor that triggers a different cascade, resulting in the activation of Phospholipase C (PLC). PLC indirectly causes the release of calcium from the hepatocytes endoplasmic reticulum into the cytosol. The ...

Sarcoplasmic vesicles and ß-glycogen particles 30-40 mµ in diameter were isolated from perfused rabbit skeletal muscle by the differential precipitation-centrifugation method. This microsomal fraction was subjected to zonal centrifugation on buffered sucrose gradients, in a B XIV Anderson type rotor, for 15 hr at 45,000 rpm in order to separate the two cytoplasmic organelles. Zonal profiles of absorbance at 280 mµ, proteins, glycogen, and enzymatic activities (phosphorylase b kinase, phosphorylase b, and glycogen synthetase) were performed. Whereas the entire synthetase activity was found combined with the glycogen particles, 39% of phosphorylase and 53% of phosphorylase b kinase activities, present in the microsomal fraction, were recovered in the purified vesicular fraction (d = 1.175). This latter fraction consists of vesicles, derived from the sarcoplasmic reticulum, and of small particles 10-20 mµ in diameter attached to the outer surface of the membranes. These particles disappear ...

Glycogen Phosphorylase: An enzyme that catalyzes the degradation of GLYCOGEN in animals by releasing glucose-1-phosphate from the terminal alpha-1,4-glycosidic bond. This enzyme exists in two forms: an active phosphorylated form ( PHOSPHORYLASE A) and an inactive un-phosphorylated form (PHOSPHORYLASE B). Both a and b forms of phosphorylase exist as homodimers. In mammals, the major isozymes of glycogen phosphorylase are found in muscle, liver and brain tissue.

Isoproterenol (0.01-10 nM) caused the rapid, complete conversion of glycogen phosphorylase from the b to the a form in cultured C-6 astrocytoma cells. This was associated with a 60-fold elevation in cellular cyclic 3,5-AMP content. Both effects were blocked stereoselectively by (-)-propranolol. The beta adrenoceptor partial agonists (±)-salbutamol (1 nM-10 µM) and (±)-hydroxybenzylpindolol (0.1 nM-10 µM) also caused full conversion of phosphorylase b to a, although their maximal effects on cellular cyclic AMP content were only 80% and 17.5%, respectively, of that obtainable with (-)-isoproterenol. Prostaglandin E1 (PGE1), which caused only a 1.6-fold elevation in cyclic AMP content, gave rise to 54% conversion of phosphorylase b to the a form. Prior incubation of cells with 3-isobutyl-1-methylxanthine caused a 1.4-fold elevation of cyclic AMP and converted 36% of phosphorylase b to the a form. Under those conditions dibutyryl cyclic AMP fully activated phosphorylase b to a , and the ...

Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA (By similarity). Essential for the efficient reshuttling of ILF3 into the nucleus (By similarity).

Order Thymidine Phosphorylase ELISA Kits for many Reactivities. Chicken, Dog, Guinea Pig and more. Compare Thymidine Phosphorylase ELISA Kits and find the right product on antibodies-online.com.

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