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  • Animals
  • Phosphorylation
  • Springer  (17)
  • American Meteorological Society
  • MDPI Publishing
  • 1990-1994  (17)
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Keywords
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Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Preparation and properties of polyamide-imides derived from 1,3-bis(4-aminophenoxy)benzene, trimellitic anhydride, and various aromatic diamines (1994)
    Springer
    Journal of polymer research 1 (1994), S. 43-49 
    Details
    ISSN: 1572-8935
    Keywords: Poly(amide-imide)s ; Polycondensation ; Phosphorylation ; Aromatic diamines ; 1,3-bis(4-aminophenoxy)benzene ; 1, 3-bis(4-trimellitimidophenoxy)benzene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract A diamine, 1,3-bis(4-aminophenoxy) benzene (II), was synthesized in two steps; fist from the condensation of resorcinol with p-chloronitrobenzene in the presence of potassium carbonate, producing I ,3-bis(4-nitrophenoxy) benzene (I), followed by hydrazine hydrate/Pd-C reduction. A two imide rings-preformed dicarboxylic acid, 1,3-bis(4-trimellitimidophenoxy)benzene (III), was prepared from the condensation of diamine II and trimellitic anhydride in 1:2 molar ratio. A series of structurally new polyamide-imides (Va-p) were directly synthesized from the diacid III and various aromatic diamines (IVa-p). The resultant polyamide-imides had inherent viscosities between 0.56–1.39 dl/g. All polymers, except some derived from diamines with p-phenoxy structure, showed excellent solubility. Some polymer resulted in tough or flexible transparent films. Dynamic TG data indicated that all polymers possess excellent thermal stability with no significant weight loss up to the temperature of approximately 450 °C in nitrogen, and their 10% weight loss temperature was recorded in the range of 489–577 °C. Measurements of wide-angle X-ray diffraction revealed that some polymers derived from p-phenoxy group-containing diamines showed crystalline patterns.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01378593
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  • 2
    Electronic Resource
    Electronic Resource
    Mass-spectrographic analysis of a porcine amelogenin identifies a single phosphorylated locus (1994)
    Springer
    Calcified tissue international 55 (1994), S. 398-400 
    Details
    ISSN: 1432-0827
    Keywords: Enamel ; Proteins ; Phosphorylation ; Amelogenins ; Tooth
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract The amelogenins of the extracellular matrix of developing dental enamel, comprise a family of tissue-specific proteins which are postulated to play a central role in the biomineralization of dental enamel [1]. The primary structures of amelogenins derived from cow, pig, human, mouse and rat have now been elucidated by the interpretation of cDNA sequences or by direct amino acid sequence determinations [2–6] demonstrating a high degree of sequence homology between species [1]. However, the nature of post-translational modification of these proteins is less clear. In particular, early reports of amelogenin phosphorylation [7–8] have proved to be difficult to confirm by direct chemical analyses [1]. Using mass spectrographic analysis, we recently [9], reported that the lower molecular weight (5–7 kDa) bovine and porcine amelogenin polypeptides (TRAP and LRAP) contained a single phospho-serine residue at position 16Ser and, since these polypeptides are derived by proteolytic processing from the higher molecular weight “parent” amelogenins (18–25 kDa), we concluded that these precursor molecules must also be phosphorylated, as has previously been suggested [10]. In contrast to these observations, an extensive amino acid sequencing study of porcine amelogenins has recently reported no evidence for such phosphorylation [11]. We now report that a new analysis of the major porcine(“20K”) amelogenin provides positive evidence for porcine amelogenin phosphorylation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00299322
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of the gap junction protein, connexin45 (1994)
    Springer
    The journal of membrane biology 139 (1994), S. 31-40 
    Details
    ISSN: 1432-1424
    Keywords: Connexin45 ; Gap junction ; Intercellular communication ; Phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Connexin45 is a gap junction protein which forms channels with unique characteristics. RNA blots demonstrated that connexin45 is expressed in a number of cell lines including WB, SK Hepl, BHK, A7r5, CLEM, and BWEM cells. Connexin45 was further studied in BWEM cells using specific affinity-purified antibodies directed against a synthetic peptide representing amino acids 285–298 of its sequence. Immunofluorescence experiments demonstrated that the BWEM cells expressed both connexin43 and connexin45 and that these connexins colocalized. Connexin45 polypeptide, immunoprecipitated from BWEM cells metabolically labeled with [35S]-methionine, consisted of a predominant 48 kD polypeptide. Connexin45 and connexin43 contained radioactive phosphate when immunoprecipitated from BWEM cells metabolically labeled with [32P]-orthophosphoric acid. This phosphate label was removed from connexin45 by alkaline phosphatase digestion. Treatment of BWEM cells with the tumor promoting agent 12-O-tetradecanoylphorbol-13-acetate (TPA) inhibited intercellular passage of microinjected Lucifer yellow. While TPA treatment induced phosphorylation of connexin43 in these cells, it reduced the expression of connexin45. Furthermore, the connexin45 expressed after TPA treatment was not phosphorylated. These results suggest that treatments which alter protein phosphorylation may regulate connexin43 and connexin45 in BWEM cells by different mechanisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00232672
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  • 4
    Electronic Resource
    Electronic Resource
    Pheromone-induced phosphorylation of antennal proteins from insects (1994)
    Springer
    Journal of comparative physiology 164 (1994), S. 76-80 
    Details
    ISSN: 1432-136X
    Keywords: Insect antennae ; Pheromones ; Second messenger ; Phosphorylation ; Moth,Heliothis virescens
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Protein kinase C inhibitors, such a calphostin C, abolish the transient nature of pheromone-induced rapid inositol 1,4,5-triphosphate (IP3) responses, suggesting that pheromone signalling is terminated by phosphorylation of specific proteins. Challenging antennal preparations fromHeliothis virescens with species-specific pheromones in the presence of [32P]-γ-ATP led to a rapid, stimulus-dependent incorporation of32Pi into antennal proteins. Pheromone-induced phosphorylation was completely abolished by a blockade of protein kinase C. Electrophoretic analysis revealed that upon stimulation with a pheromone blend two polypeptide bands were labelled; stimulation solely with the major compound (Z-11-hexadecenal) resulted in only a single labelled band. The data indicate that pheromones cause phosphorylation of specific antennal proteins which may be receptors for pheromones.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00714574
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  • 5
    Electronic Resource
    Electronic Resource
    Neurofilaments in rat and cat spinal cord; a comparative immunocytochemical study of phosphorylated and non-phosphorylated subunits (1993)
    Springer
    Cell & tissue research 272 (1993), S. 249-256 
    Details
    ISSN: 1432-0878
    Keywords: Spinal cord ; Motoneurones ; Dorsal horn ; Neurofilament ; Phosphorylation ; Immunocytochemistry ; Rat ; Cat
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Neurofilament immunoreactivity was examined in spinal cords of rats and cats with antibodies to all three subunits (68 kD, 155 kD and 200 kD) and to different phosphorylation states of 200 kD. NFHP-, an antibody against non-phosphorylated 200 kD, labelled all rat neuronal perikarya but failed to labet cat neurofilaments. In both species, the perikarya and processes of motoneurones were immunoreactive for all three subunits but most dorsal horn neuronal perikarya were not immunoreactive for 68 kD and 155 kD. Motoneuronal perikarya and proximal processes showed filamentous labelling for 68 kD but not for 155 kD in the rat, while in neither species did these show labelling with RT97, an antibody against a highly phosphorylated form of 200 kD; immunoreactivity for 200 kD was present in both filamentous (probably partially phosphorylated) and non-filamentous (non-phosphorylated) forms, but in dorsal horn neurones only the latter was present. Interpretations consistent with this data are: in rat and possibly also cat, motoneuronal neurofilaments consist of a 68 kD backbone with partially phosphorylated 200 kD sidearms, with both 155 kD and 200 kD (non-phosphorylated) subunits in a non-filamentous form; this neurofilament becomes more highly phosphorylated along the proximal processes. The dorsal horn neurones probably contain 200 kD in a non-filamentous form but may lack the other subunits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00302730
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  • 6
    Electronic Resource
    Electronic Resource
    Isolation and characterization of a phosphoprotein phosphatase type 2A gene from alfalfa (1993)
    Springer
    Molecular genetics and genomics 240 (1993), S. 126-131 
    Details
    ISSN: 1617-4623
    Keywords: Cell cycle ; Medicago sativa ; Phosphorylation ; Mitosis ; Phosphatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Phosphoprotein phosphatases are central regulatory components of the cell cycle in eukaryotes. We report the cloning and sequencing of an alfalfa phosphoprotein phosphatase type 2A (pp2aMs) cDNA. The predicted protein sequence shows high similarity to PP2A from Brassica napus, rabbit and Drosophila. No changes in pp2aMs mRNA abundance during the cell cycle were found. During growth of a batch cell culture, mRNA levels decreased gradually. In planta, all organs contained pp2a transcripts but maximal mRNA levels were detected in stems. Since Southern analysis indicated the presence of a small pp2a gene family in alfalfa, it appears that different subtypes may have specialized roles in various tissues and developmental situations which await characterization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00276891
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  • 7
    Electronic Resource
    Electronic Resource
    Osmoregulation of the fatty acid receptor gene fadL in Escherichia coli (1993)
    Springer
    Molecular genetics and genomics 240 (1993), S. 339-347 
    Details
    ISSN: 1617-4623
    Keywords: OmpR ; EnvZ ; Phosphorylation ; Transcriptional control ; DNA binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The fadL gene of Escherichia coli codes for an outer membrane protein that is involved in the uptake of long-chain fatty acids. Uptake is regulated by environmental osmolarity, and decreases when the cells are grown under conditions of high osmolarity. A temperature-sensitive mutant that requires fatty acid for growth at 42° C was unable to grow at the high temperature even in the presence of fatty acid if the medium contained 10% sucrose. Promoter activity of the fadL gene in vivo was repressed by high osmolarity in a FadR repressor null mutant. Furthermore, in vitro transcription of the fadL gene was strongly repressed by the addition of OmpR and EnvZ proteins. The results of gel retardation and DNase I protection experiments indicated that OmpR, after incubation with the protein kinase EnvZ, specifically binds to at least four sites around the fadL promoter, two upstream and two downstream from the transcriptional start site. These results suggest that transcription of the fadL gene is osmotically regulated by the OmpREnvZ two-component system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00280384
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  • 8
    Electronic Resource
    Electronic Resource
    Protein kinase C in turtle brain: changes in enzyme activity during anoxia (1993)
    Springer
    Journal of comparative physiology 163 (1993), S. 84-88 
    Details
    ISSN: 1432-136X
    Keywords: Anoxia ; Protein kinase C ; Phosphorylation ; Brain ; Turtle, Pseudemys elegans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Protein kinase C from the anoxia-tolerant turtle Pseudemys scripta elegans was investigated to determine its role in mediating changes in brain metabolism associated with anoxia. Measurements of protein kinase C distribution in cytosol and membrane-associated fractions of cerebrum and hindbrain were performed with warm (18 °C)- and cold (7 °C)-acclimated animals exposed to normoxic or anoxic conditions. In cerebrum, the percentage of bound protein kinase C decreased from 48.5% to 35.1% in warm-acclimated animals and from 45.0% to 25.6% in cold-acclimated animals. In the hind-brain, bound protein kinase C increased from 45.0% to 72.9% in warm-acclimated animals and from 40.3% to 68.8% in cold-acclimated animals. The presence of three distinct protein kinase C isozymes (Types I, II and III) was confirmed by hydroxylapatite chromatography. The distribution of isozymes between cytosolic and membrane-associated fractions in cerebrum was 24% I, 37% II and 39% III (cytosolic) and 32% I, 35% II and 34% III (membrane-associated). In the hindbrain, the protein kinase C isozyme distribution was 34% I, 40% II and 26% III (cytosolic) and 18% I, 47% II and 35% III (membrane-associated). Kinetic characterization of the three isozymes showed that Type I was 27% activated by Ca2+, whereas Types II and III were only 4% and 2% activated by Ca2+, respectively. Full activity for all enzymes was observed only in the presence of phosphatidylserine and diacylglycerol. No differences in the K m for ATP, the K a for Ca2+ or the K a for phosphatidylserine were observed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309670
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  • 9
    Electronic Resource
    Electronic Resource
    Dual role of calmodulin in excitable cells (1993)
    Springer
    Annals of biomedical engineering 21 (1993), S. 669-677 
    Details
    ISSN: 1573-9686
    Keywords: Channel ; Phosphorylation ; Calmodulin ; Membrane ; Electrostatics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Technology
    Notes: Abstract Consideration of the enzymatic reactions governing calcium channel phosphorylation and dephosphorylation leads one to deduce that there exist separate groups of enzymes, membrane-bound and cytoplasmic, that are activated by a common mediator, calmodulin (CaM), whose time-dependent appearance (via diffusion) at both locales is controlled by both intracellular calcium levels and electrostatic interaction with the membrane. In brief, the change in the sign and extent of the electrical charge borne by the modulator in the presence of calcium (Ca) brings about the electrostatic attraction that enables the transport of [Ca−CaM] to the membrane. This translocation of Ca−CaM makes possible a sequential activation of cellular enzymes whose locations differ. The sequence, both spatial and temporal, of the activation of various cellular enzymes by Ca−CaM appears to be a control network shared in common by excitable cells containing a stimulus-response pathway mediated by second messengers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02368646
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  • 10
    Electronic Resource
    Electronic Resource
    Gametophytic self-incompatibility inPapaver rhoeas L. (1992)
    Springer
    Sexual plant reproduction 5 (1992), S. 1-7 
    Details
    ISSN: 1432-2145
    Keywords: Self-incompatibility ; Papaver rhoeas ; in vitro system ; Pollen response genes ; Phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have developed an in vitro system whereby we can reproduce the self-incompatibility (SI) reactions ofP. rhoeas in pollen grown in vitro, using stigmatic extracts. This has enabled us to investigate a number of aspects of SI, which would otherwise be difficult. On the stigma side of the reaction, the in vitro system has enabled us to characterize and partially purify the stigmatic S-component, following S-specific activity. It has also enabled us to establish that, in contrast to the S-linked glycoprotein ofNicotiana alata, no detectable ribonuclease activity correlates with the presence of the functional stigmatic S-gene product in this species. Turning to look at the pollen side, we have used the in vitro system to study the metabolic events occurring in the pollen ofP. rhoeas as a consequence of the SI reaction. We have determined that it requires both de novo glyco-sylation and RNA transcription for full inhibition of pollen-tube growth during the SI reaction. Transcription products of pollen SI response genes, which are produced specificially in an incompatible reaction, have been identified. These pollen response genes have been cloned and are currently being characterized. Since the extracellular pollen-stigma interaction results directly in gene transcription in the pollen, it seems likely that a signal transduction mechanism may be operating in the SI response. The in vitro system has allowed us to begin to investigate this possibility. We have detected rapid and transient phosphorylation of certain pollen proteins, together with changes in phosphatase activity during the SI reaction. These studies provide evidence for a role for signal transduction in the SI reaction. Thus, our in vitro system has enabled us to begin to examine, not only stigma and pollen components, but also the interaction between them in the SI reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00714552
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  • 11
    Electronic Resource
    Electronic Resource
    Phosphorylation of proteins in Xanthomonas campestris pv. oryzae (1992)
    Springer
    Archives of microbiology 158 (1992), S. 262-266 
    Details
    ISSN: 1432-072X
    Keywords: Bacterium ; Phosphorylation ; Protein kinase ; Xanthomonas campestris pv. oryzae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Protein phosphorylation was studied in Xanthomonas campestris pv. oryzae in vivo and in vitro. In vitro labelling showed that the protein kinases in this bacterium used both ATP and GTP as nucleotide substrates at nearly the same efficiency. At least 6 proteins were phosphorylated in vitro, including abundant species of p81, p44, and p32 with M r of 81000, 44000, and 32000, respectively. Three types of phosphate-protein linkage were found in this bacterium: O-phosphate, N-phosphate and probably acyl phosphate. The p81 and p32 were phosphorylated at histidine. The p44 had mainly phosphoserine and a small part of phosphohistidine. The phosphorylation profile was variable depending on the growth conditions. Furthermore, by a virulent phage Xp10 infection the quantity of phosphorylation increased: for phosphohistinine more than 10-fold, and for phosphoserine about 3-fold. Thus, in this bacterium phosphorylation may be linked with a physiological regulation system and with Xp10 phage development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245242
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  • 12
    Electronic Resource
    Electronic Resource
    Phosphorylation of a putative myosin light chain inChara by calcium-dependent protein kinase (1992)
    Springer
    Protoplasma 171 (1992), S. 85-88 
    Details
    ISSN: 1615-6102
    Keywords: Ca2+-dependent protein kinase ; Chara ; Cytoplasmic streaming ; Myosin light chain ; Phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ca2+-dependent protein kinase (CDPK) has been proposed to mediate inhibition by Ca2+ of cytoplasmic streaming in the green algaChara. We have identified the in vivo substrate(s) of CDPK inChara by using vacuolar perfusion of individual internodal cells with [γ-32P]ATP. Phosphorylation of several polypeptides is enhanced when perfusions are performed at 10−4M free Ca2+ compared to 〈10−9M free Ca2+. The Ca2+-stimulated phosphorylation of these proteins is inhibited by the presence of a monoclonal antibody to soybean CDPK. One of these proteins is 16 to 18kDa and is recognized by an antibody against gizzard myosin light chains. These results demonstrate that inChara, several polypeptides are phophorylated by CDPK and one of these proteins has been tentatively identified as a myosin light chain. These observations support the hypothesis that Ca2+-regulated phosphorylation of myosin is involved in the regulation of cytoplasmic streaming.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01379284
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  • 13
    Electronic Resource
    Electronic Resource
    Single cardiac outwardly rectifying K+ channels modulated by protein kinase A and a G-protein (1991)
    Springer
    European biophysics journal 20 (1991), S. 281-286 
    Details
    ISSN: 1432-1017
    Keywords: Cardiac K+ channels ; Phosphorylation ; GTP ; GDP ; Neonatal rat heart myocytes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Elementary K+ currents were recorded at 19 °C in cell-attached and in inside-out patches excised from neonatal rat heart myocytes. An outwardly rectifying K+ channel which prevented Na+ ions from permeating could be detected in about 10% of the patches attaining (at 5 mmol/l external K+ and between − 20 mV and + 20 mV) a unitary conductance of 66 +- 3.9 pS. K (outw.-rect.) + channels have one open and at least two closed states. Open probability and τopen rose steeply on shifting the membrane potential in the positive direction, thereby tending to saturate. Open probability (at −7 mV) was as low as 3 ± 1% but increased several-fold on exposing the cytoplasmic surface to Mg-ATP (100 μmol/l) without a concomitant change of τopen. No channel activation occurred in response to ATP in the absence of cytoplasmic Mg−+. The cytoplasmic administration of the catalytic subunit of protein kinase A (120–150 μ/ml) or GTP-γ-S (100 μmol/l) caused a similar channel activation. GDP-β-S (100 μmol/l) was also tested and found to be ineffective in this respect. This suggests that cardiac K (outw.-rect.) + channels are metabolically modulated by both cAMP-dependent phosphorylation and a G-protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00450563
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  • 14
    Electronic Resource
    Electronic Resource
    Qualitative and quantitative comparison of the distribution of phosphorylated and non-phosphorylated neurofilament epitopes within central and peripheral axons of adult hamster (Mesocricetus auratus) (1991)
    Springer
    Cell & tissue research 263 (1991), S. 265-270 
    Details
    ISSN: 1432-0878
    Keywords: Neurofilaments ; Phosphorylation ; Axon ; Immunocytochemistry ; Golden syrian hamster, Mesocricetus auratus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of phosphorylated and nonphosphorylated neurofilament epitopes was determined immunocytochemically in adjacent 2 μm-thick sections of sciatic nerve, ventral root and spinal cord. Staining was scored as either intense, moderate or absent and the proportion of labeled axons was calculated for each category. Nearly all sciatic nerve and ventral root axons were immunoreactive with both antibodies against phosphorylated and non-phosphorylated neurofilaments and there were no significant differences in the number of intensely- or moderately-labeled axons. Within the spinal cord however, while the majority of large caliber axons was stained with both antibodies, there was a significant number of small caliber axons which stained only with antibodies against phosphorylated neurofilaments. These results show that phosphorylated and nonphosphorylated neurofilaments are extensively codistributed in CNS and PNS axons, and that in the CNS, staining intensity for non-phosphorylated epitopes is less in the smaller axons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00318768
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  • 15
    Electronic Resource
    Electronic Resource
    An update on fibrous flagellar roots in green algae (1991)
    Springer
    Protoplasma 164 (1991), S. 38-44 
    Details
    ISSN: 1615-6102
    Keywords: Flagellate green algae ; Fibrous flagellar roots ; System II fibres ; System I fibres ; Centrin ; Assemblin ; Phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In flagellate green algae two types of fibrous flagellar roots can be distinguished: system I fibres, cross-striated bundles of 2nm filaments (striation periodicity about 30 nm), which are associated with flagellar root microtubules, and system II fibres, contractile bundles of 4–8 nm filaments which are often cross-striated (striation periodicity variable but greater than 80 nm). The major protein of system II fibres is centrin, a Ca2+-modulated phosphoprotein, which is a member of the EF-hand protein family. The major protein of system I fibres (of severalChlamydomonas-type green algae) is a 34 kDa phosphoprotein, named assemblin. Because of the solubility characteristics of system I fibres and the properties of their major protein (paracrystal-formation in vitro, several isoelectric variants, heptad motifs in parts of the amino acid sequence), assemblin is presumably related to the k-m-e-f class of α-helical fibrous proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01320813
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  • 16
    Electronic Resource
    Electronic Resource
    Purification of macrolide 2′-phosphotransferase fromStreptomyces coelicolor Müller (1990)
    Springer
    Journal of industrial microbiology and biotechnology 6 (1990), S. 295-297 
    Details
    ISSN: 1476-5535
    Keywords: Phosphorylation ; Oleandomycin ; Macrolide 2′-phosphotransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An enzyme that catalyzes 2′-O-phosphorylation of oleandomycin and several other macrolide antibiotics has been purified approximately 47-fold from cell-free extracts ofStreptomyces coelicolor Müller, NRRL 3532 (UC™ 5240). The reaction product was verified as being oleandomycin-2′-O-phosphate by mass spectrometry. As a result of purification, the enzyme was separated from two lincosaminide inactivating enzyme activities also present in the cell-free extract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01575877
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  • 17
    Electronic Resource
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    Characterization of a GDP-sensitive phosphorylation in plasma membranes ofD. discoideum (1990)
    Springer
    The protein journal 9 (1990), S. 417-425 
    Details
    ISSN: 1573-4943
    Keywords: Phosphorylation ; GDP-stimulated ; developmental regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In a previous study, we reported the GDP-dependent phosphorylation of a 36 kD membrane protein, p36, inD. discoideum membranes prepared from starved (aggregation competent) cells (Anschutzet al., 1989). Here we show that p36 can be phosphorylated when membranes are supplied either ATP or GTP as the phosphate donor, but that a greater level of p36 phosphorylation is achieved with GTP. The rate of phosphorylation of p36, using either nucleotide triphosphate, is enhanced by GDP. This reflects a decrease in the apparentK m of the enzyme for the particular nucleotide triphosphate. p36 can also be phosphorylated in membranes prepared from vegetative cells. However, the ability of GDP to stimulate p36 phosphorylation is not observed in vegetative cell membranes. Competition experiments indicate that there are also developmental differences in the nucleotide triphosphate site(s) available to phosphorylate p36.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024617
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