Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Protamine Kinase”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 793 records · Page 44Linked to original sources
PubMed2004

First combined cladistic analysis of marsupial mammal interrelationships.

We combine osteological, dental, and soft tissue data with sequences from three nuclear and five mitochondrial genes, sampling all major living clades of marsupials plus several extinct taxa, to perform a simultaneous analysis of marsupial interrelationships. These data were analyzed using direct optimization and sensitivity analysis on a parallel supercomputing cluster, and compared with trees produced with conventional parsimony and likelihood algorithms using a static alignment. A major issue in marsupial phylogeny is the relationships among australidelphians. Optimal analyses using direct optimization and those based on the static alignment support the basal positions of peramelians (bandicoots) and Dromiciops ('monito del monte') within Australidelphia, and in all but one case these analyses support a monophyletic Eometatheria, a group consisting of all australidelphians excluding peramelians. Dromiciops is basal within Eometatheria in analyses that maximize congruence across partitions, including the equally weighted parameter set. The topologies resulting from direct optimization under all parameter sets show some differences, but all show a high degree of resolution. Direct optimization supports high-level clades supported by analyses of partitioned molecular (e.g., Notoryctes as sister group of Dasyuromorphia) and morphological (e.g., Diprotodontia) data.

Animals↗
PubMed1975

Separation of "estrogen-induced" protein from phosphoprotein phosphatase activity of immature rat uterus.

Preparations of the "induced protein" which appears in the rat uterus within 40 min of estradiol administration have recently been reported to contain phosphoprotein phosphatase (phosphoprotein phosphohydrolase, EC 3.1.3.16) activity. We found that these two proteins distribute differently on ammonium sulfate fractionation of uterine cytosol. Preparative cellulose acetate electrophoresis afforded complete (greater than 99.9%) separation of phosphoprotein phosphatase activity from the induced protein. The specific activity of phosphoprotein phosphatase in uterine cytosol was unchanged 1, 4, 12, or 24 hr after estradiol administration. These results are incompatible with the view that the induced protein mediates estrogen action by virtue of an inherent phosphoprotein phosphatase activity.

Animals↗
PubMed1984

Purification and properties of branched-chain alpha-keto acid dehydrogenase phosphatase from bovine kidney.

Branched-chain alpha-keto acid dehydrogenase (BCKDH) phosphatase was purified about 8000-fold from extracts of bovine kidney mitochondria. The highly purified phosphatase exhibited a molecular weight of approximately 460,000, as estimated by gel-permeation chromatography. Another form of the phosphatase, with an apparent molecular weight of approximately 230,000, was also detected under conditions of high dilution. In contrast to pyruvate dehydrogenase phosphatase, BCKDH phosphatase was active in the absence of divalent cations. BCKDH phosphatase was inactive toward 32P-labeled phosphorylase a, but exhibited approximately 10% maximal activity with 32P-labeled pyruvate dehydrogenase complex. BCKDH phosphatase activity was inhibited by GTP, GDP, ATP, ADP, UTP, UDP, CTP, and CDP. Half-maximal inhibition occurred at about 60, 200, 200, 400, 100, 250, 250, and 400 microM, respectively. These inhibitions were reversed completely by 2 mM Mg2+. GTP was replaceable by guanosine 5'-(beta, gamma-imido)triphosphate. GMP, AMP, UMP, CMP, NAD, and NADH showed little effect, if any, on BCKDH phosphatase activity at concentrations up to 1 mM. Heparin showed half-maximal inhibition at 2 micrograms/ml. This inhibition was only partially (30%) reversed by 2 mM Mg2+. CoA and various acyl-CoA compounds exhibited half-maximal inhibition at 150-300 microM. These inhibitions were not reversed by 2 mM Mg2+. BCKDH phosphatase activity was stimulated 1.5- to 3-fold by protamine, poly(L-lysine), and poly(L-arginine) at 3.6 micrograms/ml.

3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)↗
PubMed1985

Casein and histone kinases of a rat ascites hepatoma as compared with those of rat liver.

Seryl/threonyl-protein kinases in cytosolic and particulate fractions from rat liver and AH-13, a rat ascites hepatoma, have been studied by chromatographing these fractions on DEAE-cellulose and assaying the eluates with casein, phosvitin, histone and protamine as substrates. Liver cytosolic fraction contains a group of well-characterized seryl/threonyl-protein kinases, namely, casein kinases I and II and histone kinases I and II. Liver particulate fraction, on the other hand, is almost totally devoid of casein kinase I and histone kinase I but contains an additional peak of casein kinase tentatively designated casein kinase III. In AH-13, cytosolic casein kinase I is markedly increased and particulate-associated casein kinases II and III are moderately increased as compared with liver. Moreover, it was found that in AH-13, the histone kinase I level is high in the particulate fraction but markedly decreased in the cytosolic fraction. It is suggested that particulate-associated histone kinase I may be of cytosolic origin.

Animals↗
PubMed1987

Properties of poliovirus associated protein kinase.

Highly purified virulent poliovirus preparations harbour an endogenous protein kinase. Enzyme activity increases significantly upon purification of infectious virus particles from infected HeLa cells. Enzyme activity is stimulated by divalent cations. The substrate specificity and the degree of stimulation of the kinase are dependent on the nature of the divalent cations included in the assay. The preferred substrates for this kinase are the viral capsid proteins. Exogenously added proteins such as alpha-casein, phosvitin and protamine are also phosphorylated by the kinase. Moreover, these proteins enhance the phosphorylation of viral proteins. In the presence of Mg++ VP 2 and VP 0 are highly phosphorylated, while in the presence of Zn++ only VP 2 and VP 4, but not VP 0 or exogenous proteins are phosphorylated. Poliovirus associated protein kinase exhibits optimal activity at pH 7.9 in the presence of 10 mM Mg++. The Km for ATP is shown to be 40 microM. By testing different nucleotides as phosphate donors a specificity of the phosphorylation reaction for ATP is demonstrated. Phosphoamino acid analysis of hydrolysates of the substrates phosphorylated in the presence of Mg++ by thin layer electrochromatography and HPLC yielded phosphoserine and phosphothreonine from viral capsid proteins while hydrolysates of protamine yield only phosphoserine. Destabilization of the viral capsid, e.g. by preincubation at 42 degrees C for 20 minutes results in a stimulation of kinase activity. Moreover, phosphorylation of the poliovirus capsid proteins itself results in destabilization of the viral capsid. These findings suggest that phosphorylation of the viral coat proteins triggers or enhances the uncoating of poliovirus leading to the release of viral RNA.

Amino Acids↗
PubMed1985

[Regulatory properties of phosphorylase from chicken skeletal muscle].

The main kinetic parameters for purified phosphorylase kinase from chicken skeletal muscle were determined at pH 8.2: Vm = 18 micromol/min/mg; apparent Km values for ATP and phosphorylase b from rabbit muscle were 0.20 and 0.02 mM, respectively. The activity ratio at pH 6.8/8.2 was 0.1-0.4 for different preparations of phosphorylase kinase. Similar to the rabbit enzyme, chicken phosphorylase kinase had an absolute requirement for Ca2+ as demonstrated by complete inhibition in the presence of EGTA. Half-maximal activation occurred at [Ca2+] = 0.4 microM at pH 7.0. In the presence of Ca2+, the chicken enzyme from white and red muscles was activated 2-4-fold by saturating concentrations of calmodulin and troponin C. The C0.5 value for calmodulin and troponin C at pH 6.8 was 2 and 100 nM, respectively. Similar to rabbit phosphorylase kinase, the chicken enzyme was stimulated about 3-6-fold by glycogen at pH 6.8 and 8.2 with half-maximal stimulation occurring at about 0.15% glycogen. Protamine caused 60% inhibition of chicken phosphorylase kinase at 0.8 mg/ml. ADP (3 mM) at 0.05 mM ATP caused 85% inhibition with Ki = 0.2 mM. Unlike rabbit phosphorylase kinase, no phosphorylation of the chicken enzyme occurred in the presence of the catalytic subunit of cAMP-dependent protein kinase. Incubation with trypsin caused 2-fold activation of the chicken enzyme.

Adenosine Diphosphate↗
PubMed1981

Identification of a protein kinase activity in purified foot- and-mouth disease virus.

Purified preparations of foot-and-mouth disease virus types A, O, and C contain a protein kinase activity which can transfer the gamma phosphate of [32P]ATP to virion structural proteins VP2 and VP3 and exogenous acceptor proteins. Utilizing protamine sulfate as an acceptor, the kinase activity can be demonstrated in disrupted virus but not in intact virus. The enzyme is heat labile with optimal activity at pH 7 or greater. Serine residues of protamine sulfate were identified as the amino acid phosphorylated by the protein kinase. Treatment of purified virus with trypsin, which cleaves VP3, did not affect the protein kinase activity. The results indicate that the protein kinase activity found in FMDV is present in an internally located protein of viral or host origin.

Adenosine Triphosphate↗
PubMed1976

Independent modulation of hepatic protein kinase activities.

The effects of hormonal status on protein kinase activity was examined in homogenates of rat liver. Protein kinase activity was evaluated from incorporation of 32P from [gamma-32P]ATP into protamine or histone as receptor substrates. Protamine phosphorylation in the presence or absence of cyclic AMP exceeded histone phosphorylation by at least a factor or two. Hypophysectomy markedly increased protamine phosphorylation in the presence or absence of saturating amounts of cyclic AMP. In contrast, hypophysectomy only slightly increased cyclic AMP independent phosphorylation of histone. These results could not be amounted for by differences in ATPase or protein phosphase activities. Cortisone (2 mg/day x 3) decreased total protein kinase activity in livers of hypophysectomized rats when protamine was substrate, but had no effect on the total activity toward histone. Growth hormone (100 mug/day x 3) significantly increased histone, but not protamine phosphorylation in livers of hypophysectomized rats. Administration of 5 mug of triiodothyonine/day to hypophysectomized rats also markedly increased the phosphorylation of histone, but not protamine when saturating amounts of cyclic AMP were present. These results support the hypothesis that liver may contain more than one type of protein kinase activity and that the different protein kinase activities can be separately affected by hormones. Such control distal to cyclic AMP might allow selective modulation of cyclic AMP-dependent processes in cells which carry out more than one such process.

Adenosine Triphosphatases↗
PubMed1980

Biochemical studies of the excitable membrane of Paramecium. IV. Protein kinase activities of cilia and ciliary membrane.

Two protein kinases (ATP: protein phosphotransferase, EC 2.7.1.37) were detected in disrupted cilia of Paramecium tetraurelia. One of the enzymes exhibited maximum activity at pH 6.0, required 4 mM Mg2+ for its maximum activity and was stimulated by cyclic AMP and cyclic GMP. Histone was a good exogenous protein substrate for this enzyme, but protamine sulfate was not. The other protein kinase showed a peak of activity at pH 8.0, required 10 mM Mg2+ for its maximum activity and was slightly inhibited by cyclic AMP and cyclic GMP. Protamine sulfate was a good exogenous substrate for this enzyme. The pH 8.0 activity partitioned preferentially with the axonemes, but the pH 6.0 activity was divided almost equally between the axonemes and the membranes. We also found indirect evidence for the presence in cilia of phosphoprotein phosphatase (phosphoprotein phosphohydrolase, EC 3.1.3.16) and adenyl cyclase (ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1) activity.

Adenosine Triphosphate↗
PubMed2004

Activation of C-kinase eta through its cholesterol-3-sulfate-dependent phosphorylation by casein kinase I in vitro.

The physiological correlation between casein kinase I (CK-I) and an isoform eta of protein kinase C (C-kinase eta) was investigated in vitro, since it has been reported that (i) cholesterol-3-sulfate (CH-3S) effectively activates C-kinase eta rather than the other isoforms (C-kinase epsilon and C-kinase delta) in vitro; and (ii) CK-I efficiently phosphorylates CH-3S-binding proteins, such as high mobility group protein 1 (HMG1), in the presence of CH-3S in vitro. We found that (i) CK-I phosphorylated Thr in preference to Ser on recombinant human C-kinase isoform eta (rhC-kinase eta) in the presence of CH-3S; (ii) this phosphorylation was selectively inhibited by CK-I-7 (a CK-I inhibitor); and (iii) the activity (phosphorylation of protamine sulfate) of rhC-kinase eta was approx. 3.2-fold stimulated by its full phosphorylation by CK-I in the presence of 3 microM CH-3S. These results suggest that CK-I is a protein kinase responsible for the activation of rhC-kinase eta in the presence of CH-3S in vitro.

Animals↗
PubMed1978

Thyroid plasma membrane-associated protein kinases: properties and substrates of solubilized and insoluble enzymes.

The protein kinase activities of thyroid plasma membranes were characterized after treatment by the nonionic detergent, Triton X-100. With endogenous substrate the protein kinase activity of intact plasma membranes appeared to be cAMP independent, whereas the solubilized plasma membranes contained a cAMP-dependent protein kinase. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of intact plasma membranes demonstrated approximately 30 protein bands, of which several were substrates for endogenous protein kinase, cAMP had a slight, but reproducible, stimulatory effect on some of these. In solubilized plasma membranes cAMP significantly augmented phosphorylation of at least seven of these proteins. Solubilized plasma membranes bound significantly more cAMP per mg protein than intact plasma membranes. The inability to unequivocally detect cAMP-dependent protein kinase in intact membranes using endogenous substrate probably reflects the much greater activity of the cAMP-independent enzyme activity. The protein kinase activity of intact plasma membranes which was stimulated by cAMP when histone was the substrate was primarily recovered in the solubilized plasma membranes. Most of the protein kinase activity of the intact plasma membranes was insoluble and was not augmented by cAMP. The solubilized protein kinase demonstrated the same Km values for ATP, cAMP, and MgCl2 as did the cytosolic protein kinase of the thyroid. Cytosolic and solubilized protein kinase activities were more sensitive to cAMP and cGMP stimulation when histone and protamine were used as substrates. Both enzyme activities were depressed by protein kinase modulator when histone, but not protamine and casein, were used as substrates. The protein kinase activity of insoluble plasma membranes was not inhibited by the protein kinase modulator.

Adenosine Triphosphate↗
PubMed1977

Increased activity of rat liver nucleolar protein kinase following triiodothyronine administration.

Triiodothyronine (T3) administration to thyroidectomized rats induces a significant increase in the nucleolus-associated protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) activity. The general properties of the protein kinase solubilized from liver nucleoli have been investigated. Mg2+ (20 mM) is essential for the reaction and an appropriate concentration of NaCl (100 mM) is required to achieve maximal phosphorylation rates. The optimal pH for casein phosphorylation is 7.6. The kinase phosphorylates casein more efficiently than phosvitin and displays an almost undetectable activity towards histones and protamine. No significant stimulation of the kinase activity by cyclic AMP has been detected. The apparent Km values for casein and ATP are 1.5 mg/ml and 1.5-10(-5) M, respectively, and are not affected by the hormone administration.

Animals↗