Muller H

References (13)

Title : Recovery of hydroxytyrosol from olive mill wastewater using the promiscuous hydrolase\/acyltransferase PestE - Terholsen_2022_Chembiochem_23_e202200254
Author(s) : Terholsen H , Kaur J , Kaloudis N , Staudt A , Muller H , Pavlidis IV , Bornscheuer U
Ref : Chembiochem , 23 :e202200254 , 2022
Abstract : Olive mill wastewater (OMWW) is produced annually during olive oil extraction and contains most of the health-promoting 3-hydroxytyrosol of the olive fruit. To facilitate its recovery, enzymatic transesterification of hydroxytyrosol (HT) was directly performed in an aqueous system in the presence of ethyl acetate, yielding a 3-hydroxytyrosol acetate rich extract. For this, the promiscuous acyltransferase from Pyrobaculum calidifontis VA1 (PestE) was engineered by rational design. The best mutant for the acetylation of hydroxytyrosol PestE_I208A_L209F_N288A was immobilized on EziG2 beads, resulting in hydroxytyrosol conversions between 82 and 89% in one hour, for at least ten reaction cycles in a buffered hydroxytyrosol solution. Due to inhibition by other phenols in OMWW the conversions of hydroxytyrosol from this source were between 51 and 62%. In a preparative scale reaction, 13.8 mg (57%) of 3-hydroxytyrosol acetate was extracted from 60 mL OMWW.
ESTHER : Terholsen_2022_Chembiochem_23_e202200254
PubMedSearch : Terholsen_2022_Chembiochem_23_e202200254
PubMedID: 35579388
Gene_locus related to this paper: pyrca-PCEST

Title : Rational Design for Enhanced Acyltransferase Activity in Water Catalyzed by the Pyrobaculum calidifontis VA1 Esterase - Staudt_2021_Microorganisms_9_1790
Author(s) : Staudt A , Terholsen H , Kaur J , Muller H , Godehard SP , Itabaiana I, Jr. , Leal ICR , Bornscheuer UT
Ref : Microorganisms , 9 :1790 , 2021
Abstract : Biocatalytic transesterification is commonly carried out employing lipases in anhydrous organic solvents since hydrolases usually prefer hydrolysis over acyl transfer in bulk water. However, some promiscuous acyltransferases can catalyze acylation in an aqueous solution. In this study, a rational design was performed to enhance the acyltransferase selectivity and substrate scope of the Pyrobaculum calidifontis VA1 esterase (PestE). PestE wild type and variants were applied for the acylation of monoterpene alcohols. The mutant PestE_I208A is selective for (-)-menthyl acetate (E-Value = 55). Highly active acyltransferases were designed, allowing for complete conversion of (-)-citronellol to citronellyl acetate. Additionally, carvacrol was acetylated but with lower conversions. To the best of our knowledge, this is the first example of the biocatalytic acylation of a phenolic alcohol in bulk water. In addition, a high citronellol conversion of 92% was achieved with the more environmentally friendly and inexpensive acyl donor ethyl acetate using PestE_N288F as a catalyst. PestE_N288F exhibits good acyl transfer activity in an aqueous medium and low hydrolysis activity at the same time. Thus, our study demonstrates an alternative synthetic strategy for acylation of compounds without organic solvents.
ESTHER : Staudt_2021_Microorganisms_9_1790
PubMedSearch : Staudt_2021_Microorganisms_9_1790
PubMedID: 34442869
Gene_locus related to this paper: pyrca-PCEST

Title : Efficient Acylation of Sugars and Oligosaccharides in Aqueous Environment Using Engineered Acyltransferases - Godehard_2021_ACS.Catal_11_2831
Author(s) : Godehard SP , Muller H , Badenhorst CPS , Stanetty C , Suster C , Mihovilovic MD , Bornscheuer UT
Ref : ACS Catal , 11 :2831 , 2021
Abstract : A major challenge for the enzymatic synthesis of sugar esters is the low solubility of sugars in anhydrous, often toxic, organic solvents. We overcame this limitation by using acyltransferases for efficient acetylation of sugars in water. Selective 6-O-acetylation of glucose, maltose, and maltotriose with conversions of up to 78% was achieved within 15 min using engineered acyltransferases (4 microM). Moreover, we identified EstA as a promiscuous acyltransferase preferentially acetylating sugars instead of hydrophobic acyl acceptors. This expands the applicability of promiscuous acyltransferases to sugar modifications and contributes to the understanding of how to adapt acyltransferases to hydrophilic substrates.
ESTHER : Godehard_2021_ACS.Catal_11_2831
PubMedSearch : Godehard_2021_ACS.Catal_11_2831

Title : Discovery and Design of Family VIII Carboxylesterases as Highly Efficient Acyltransferases - Muller_2021_Angew.Chem.Int.Ed.Engl_60_2013
Author(s) : Muller H , Godehard SP , Palm GJ , Berndt L , Badenhorst CPS , Becker AK , Lammers M , Bornscheuer UT
Ref : Angew Chem Int Ed Engl , 60 :2013 , 2021
Abstract : Promiscuous acyltransferase activity is the ability of certain hydrolases to preferentially catalyze acyl transfer over hydrolysis, even in bulk water. However, poor enantioselectivity, low transfer efficiency, significant product hydrolysis, and limited substrate scope represent considerable drawbacks for their application. By activity-based screening of several hydrolases, we identified the family VIII carboxylesterase, EstCE1, as an unprecedentedly efficient acyltransferase. EstCE1 catalyzes the irreversible amidation and carbamoylation of amines in water, which enabled the synthesis of the drug moclobemide from methyl 4-chlorobenzoate and 4-(2-aminoethyl)morpholine (ca. 20% conversion). We solved the crystal structure of EstCE1 and detailed structure-function analysis revealed a three-amino acid motif important for promiscuous acyltransferase activity. Introducing this motif into an esterase without acetyltransferase activity transformed a "hydrolase" into an "acyltransferase".
ESTHER : Muller_2021_Angew.Chem.Int.Ed.Engl_60_2013
PubMedSearch : Muller_2021_Angew.Chem.Int.Ed.Engl_60_2013
PubMedID: 33140887

Title : Recent Insights and Future Perspectives on Promiscuous Hydrolases\/Acyltransferases - Muller_2021_ACS.Catal_11_14906
Author(s) : Muller H , Terholsen H , Godehard SP , Badenhorst CPS , Bornscheuer UT
Ref : ACS Catal , 11 :12864 , 2021
Abstract : Promiscuous hydrolases/acyltransferases have attracted attention for their ability to efficiently catalyze selective transacylation reactions in water to produce esters, thioesters, amides, carbonates, and carbamates. Promiscuous hydrolases/acyltransferases can be implemented into aqueous enzyme cascades and are ideal biocatalysts for the acylation of hydrophilic substrates that are barely soluble in dry organic solvents. This activity was thought to be rare, and recent research has focused on just a small number of accidentally identified promiscuous hydrolases/acyltransferases. High-throughput screening for acyltransferases and an in silico sequence-based method for prediction of acyltransferase activity provided access to many efficient promiscuous hydrolases/acyltransferases, thereby demonstrating that promiscuous acyltransferase activity is rather common in hydrolases. These synthetically valuable enzymes could further be enhanced by protein engineering. This Perspective aims to demonstrate the synthetic potential of these enzymes and raise awareness of the frequency of this activity.
ESTHER : Muller_2021_ACS.Catal_11_14906
PubMedSearch : Muller_2021_ACS.Catal_11_14906

Title : Sequence-Based Prediction of Promiscuous Acyltransferase Activity in Hydrolases - Muller_2020_Angew.Chem.Int.Ed.Engl_59_11607
Author(s) : Muller H , Becker AK , Palm GJ , Berndt L , Badenhorst CPS , Godehard SP , Reisky L , Lammers M , Bornscheuer U
Ref : Angew Chem Int Ed Engl , 59 :11607 , 2020
Abstract : Certain hydrolases preferentially catalyze acyl transfer over hydrolysis in an aqueous environment. However, molecular and structural reasons for this phenomenon are still unclear. Here we provide evidence that acyltransferase activity in esterases highly correlates with the hydrophobicity of the substrate-binding pocket. A hydrophobicity scoring system developed in this work allows accurate prediction of promiscuous acyltransferase activity solely from the amino acid sequence of the cap domain. This concept was experimentally verified by systematic investigation of several homologous esterases, leading to the discovery of five novel promiscuous acyltransferases. We also developed a simple, yet versatile, colorimetric assay for rapid characterization of novel acyltransferases. This study demonstrates that promiscuous acyltransferase activity is not as rare as previously thought and provides access to a vast number of novel acyltransferases with diverse substrate specificities and potential applications.
ESTHER : Muller_2020_Angew.Chem.Int.Ed.Engl_59_11607
PubMedSearch : Muller_2020_Angew.Chem.Int.Ed.Engl_59_11607
PubMedID: 32243661
Gene_locus related to this paper: 9bact-Est8.6Y9K

Title : Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate - Palm_2019_Nat.Commun_10_1717
Author(s) : Palm GJ , Reisky L , Bottcher D , Muller H , Michels EAP , Walczak MC , Berndt L , Weiss MS , Bornscheuer UT , Weber G
Ref : Nat Commun , 10 :1717 , 2019
Abstract : The extreme durability of polyethylene terephthalate (PET) debris has rendered it a long-term environmental burden. At the same time, current recycling efforts still lack sustainability. Two recently discovered bacterial enzymes that specifically degrade PET represent a promising solution. First, Ideonella sakaiensis PETase, a structurally well-characterized consensus alpha/beta-hydrolase fold enzyme, converts PET to mono-(2-hydroxyethyl) terephthalate (MHET). MHETase, the second key enzyme, hydrolyzes MHET to the PET educts terephthalate and ethylene glycol. Here, we report the crystal structures of active ligand-free MHETase and MHETase bound to a nonhydrolyzable MHET analog. MHETase, which is reminiscent of feruloyl esterases, possesses a classic alpha/beta-hydrolase domain and a lid domain conferring substrate specificity. In the light of structure-based mapping of the active site, activity assays, mutagenesis studies and a first structure-guided alteration of substrate specificity towards bis-(2-hydroxyethyl) terephthalate (BHET) reported here, we anticipate MHETase to be a valuable resource to further advance enzymatic plastic degradation.
ESTHER : Palm_2019_Nat.Commun_10_1717
PubMedSearch : Palm_2019_Nat.Commun_10_1717
PubMedID: 30979881
Gene_locus related to this paper: idesa-mheth

Title : Genome Sequence of Serratia plymuthica Strain S13, an Endophyte with Germination- and Plant-Growth-Promoting Activity from the Flower of Styrian Oil Pumpkin - Muller_2013_Genome.Announc_1_e00594
Author(s) : Muller H , Furnkranz M , Grube M , Berg G
Ref : Genome Announc , 1 : , 2013
Abstract : The bacterium Serratia plymuthica strain S13 was demonstrated to colonize various plant-associated microhabitats and to suppress damping-off diseases. The completed genome sequence has a size of 5.5 Mb, containing 4,957 putative protein-encoding regions, and will be used to identify genetic determinants enabling the bacterium to escort a plant's entire life cycle.
ESTHER : Muller_2013_Genome.Announc_1_e00594
PubMedSearch : Muller_2013_Genome.Announc_1_e00594
PubMedID: 23929484
Gene_locus related to this paper: sersa-g0bfi6 , serpl-i3aik7 , serpl-s4yi15 , serpl-s4ynh7

Title : Complete Genome Sequence of the Sugar Beet Endophyte Pseudomonas poae RE*1-1-14, a Disease-Suppressive Bacterium - Muller_2013_Genome.Announc_1_e0002013
Author(s) : Muller H , Zachow C , Alavi M , Tilcher R , Krempl PM , Thallinger GG , Berg G
Ref : Genome Announc , 1 :e0002013 , 2013
Abstract : The endophytic bacterium Pseudomonas poae RE*1-1-14 shows broad antagonistic activity and is applied to seeds as a biocontrol agent to suppress late root rot in the sugar beet. The completely sequenced 5.5-Mb genome reveals genes that putatively contribute to this antagonistic activity and the intimate plant-microbe interaction.
ESTHER : Muller_2013_Genome.Announc_1_e0002013
PubMedSearch : Muller_2013_Genome.Announc_1_e0002013
PubMedID: 23516179
Gene_locus related to this paper: psefl-e2xn15 , 9psed-m4k1c1 , psefs-c3k813 , psefl-e2xkc8 , psefl-l7hkx4

Title : The complex structure of polyhydroxybutyrate (PHB) granules: four orthologous and paralogous phasins occur in Ralstonia eutropha - Potter_2004_Microbiology_150_2301
Author(s) : Potter M , Muller H , Reinecke F , Wieczorek R , Fricke F , Bowien B , Friedrich B , Steinbuchel A
Ref : Microbiology , 150 :2301 , 2004
Abstract : Analysis of the genome sequence of the polyhydroxyalkanoate- (PHA) accumulating bacterium Ralstonia eutropha strain H16 revealed three homologues (PhaP2, PhaP3 and PhaP4) of the phasin protein PhaP1. PhaP1 is known to constitute the major component of the layer at the surface of poly(3-hydroxybutyrate), poly(3HB), granules. PhaP2, PhaP3 and PhaP4 exhibited 42, 49 and 45 % identity or 61, 62 and 63 % similarity to PhaP1, respectively. The calculated molecular masses of PhaP1, PhaP2, PhaP3 and PhaP4 were 20.0, 20.2, 19.6 and 20.2 kDa, respectively. RT-PCR analysis showed that phaP2, phaP3 and phaP4 were transcribed under conditions permissive for accumulation of poly(3HB). 2D PAGE of the poly(3HB) granule proteome and analysis of the detected proteins by MALDI-TOF clearly demonstrated that PhaP1, PhaP3 and PhaP4 are bound to the poly(3HB) granules in the cells. PhaP3 was expressed at a significantly higher level in PhaP1-negative mutants. Occurrence of an unknown protein with an N-terminal amino-acid sequence identical to that of PhaP2 in crude cellular extracts of R. eutropha had previously been shown by others. Although PhaP2 could not be localized in vivo on poly(3HB) granules, in vitro experiments clearly demonstrated binding of PhaP2 to these granules. Further analysis of complete or partial genomes of other poly(3HB)-accumulating bacteria revealed the existence of multiple phasin homologues in Ralstonia solanacearum, Burkholderia fungorum and Azotobacter vinelandii. These new and unexpected findings should affect our current models of PHA-granule structure and may also have a considerable impact on the establishment of heterologous production systems for PHAs.
ESTHER : Potter_2004_Microbiology_150_2301
PubMedSearch : Potter_2004_Microbiology_150_2301
PubMedID: 15256572
Gene_locus related to this paper: alceu-q6ec20

Title : Genome evolution in yeasts - Dujon_2004_Nature_430_35
Author(s) : Dujon B , Sherman D , Fischer G , Durrens P , Casaregola S , Lafontaine I , De Montigny J , Marck C , Neuveglise C , Talla E , Goffard N , Frangeul L , Aigle M , Anthouard V , Babour A , Barbe V , Barnay S , Blanchin S , Beckerich JM , Beyne E , Bleykasten C , Boisrame A , Boyer J , Cattolico L , Confanioleri F , de Daruvar A , Despons L , Fabre E , Fairhead C , Ferry-Dumazet H , Groppi A , Hantraye F , Hennequin C , Jauniaux N , Joyet P , Kachouri R , Kerrest A , Koszul R , Lemaire M , Lesur I , Ma L , Muller H , Nicaud JM , Nikolski M , Oztas S , Ozier-Kalogeropoulos O , Pellenz S , Potier S , Richard GF , Straub ML , Suleau A , Swennen D , Tekaia F , Wesolowski-Louvel M , Westhof E , Wirth B , Zeniou-Meyer M , Zivanovic I , Bolotin-Fukuhara M , Thierry A , Bouchier C , Caudron B , Scarpelli C , Gaillardin C , Weissenbach J , Wincker P , Souciet JL
Ref : Nature , 430 :35 , 2004
Abstract : Identifying the mechanisms of eukaryotic genome evolution by comparative genomics is often complicated by the multiplicity of events that have taken place throughout the history of individual lineages, leaving only distorted and superimposed traces in the genome of each living organism. The hemiascomycete yeasts, with their compact genomes, similar lifestyle and distinct sexual and physiological properties, provide a unique opportunity to explore such mechanisms. We present here the complete, assembled genome sequences of four yeast species, selected to represent a broad evolutionary range within a single eukaryotic phylum, that after analysis proved to be molecularly as diverse as the entire phylum of chordates. A total of approximately 24,200 novel genes were identified, the translation products of which were classified together with Saccharomyces cerevisiae proteins into about 4,700 families, forming the basis for interspecific comparisons. Analysis of chromosome maps and genome redundancies reveal that the different yeast lineages have evolved through a marked interplay between several distinct molecular mechanisms, including tandem gene repeat formation, segmental duplication, a massive genome duplication and extensive gene loss.
ESTHER : Dujon_2004_Nature_430_35
PubMedSearch : Dujon_2004_Nature_430_35
PubMedID: 15229592
Gene_locus related to this paper: canga-apth1 , canga-ppme1 , canga-q6fik7 , canga-q6fiv5 , canga-q6fiw8 , canga-q6fj11 , canga-q6fjh6 , canga-q6fjl0 , canga-q6fjr8 , canga-q6fkj6 , canga-q6fkm9 , canga-q6fku7 , canga-q6fl14 , canga-q6flb5 , canga-q6fle9 , canga-q6flk8 , canga-q6fly1 , canga-q6fly9 , canga-q6fmz4 , canga-q6fnx4 , canga-q6fp28 , canga-q6fpa8 , canga-q6fpi6 , canga-q6fpv7 , canga-q6fpw6 , canga-q6fqj3 , canga-q6fr97 , canga-q6frt7 , canga-q6ftm9 , canga-q6ftu0 , canga-q6ftv9 , canga-q6ftz9 , canga-q6fuf8 , canga-q6fv41 , canga-q6fvu3 , canga-q6fw36 , canga-q6fw94 , canga-q6fwk6 , canga-q6fwm0 , canga-q6fxc7 , canga-q6fxd7 , debha-apth1 , debha-atg15 , debha-b5rtk1 , debha-b5rub4 , debha-b5rue8 , debha-b5rue9 , debha-bna7 , debha-ppme1 , debha-q6bgx3 , debha-q6bh69 , debha-q6bhb8 , debha-q6bhc1 , debha-q6bhd0 , debha-q6bhj7 , debha-q6bi97 , debha-q6biq7 , debha-q6bj53 , debha-q6bkd8 , debha-q6bks1 , debha-q6bky4 , debha-q6bm63 , debha-q6bmh3 , debha-q6bn89 , debha-q6bnj6 , debha-q6bp08 , debha-q6bpb4 , debha-q6bpc0 , debha-q6bpc6 , debha-q6bq10 , debha-q6bq11 , debha-q6bqd9 , debha-q6bqj6 , debha-q6br33 , debha-q6br93 , debha-q6brg1 , debha-q6brw7 , debha-q6bs23 , debha-q6bsc3 , debha-q6bsl8 , debha-q6bsx6 , debha-q6bta5 , debha-q6bty5 , debha-q6btz0 , debha-q6bu73 , debha-q6buk9 , debha-q6but7 , debha-q6bvc4 , debha-q6bvg4 , debha-q6bvg8 , debha-q6bvp4 , debha-q6bw82 , debha-q6bxr7 , debha-q6bxu9 , debha-q6bym5 , debha-q6byn7 , debha-q6bzj8 , debha-q6bzk2 , debha-q6bzm5 , klula-apth1 , klula-ppme1 , klula-q6cin9 , klula-q6ciu6 , klula-q6cj47 , klula-q6cjc8 , klula-q6cjq9 , klula-q6cjs1 , klula-q6cjv9 , klula-q6ckd7 , klula-q6ckk4 , klula-q6ckx4 , klula-q6cl20 , klula-q6clm1 , klula-q6cly8 , klula-q6clz7 , klula-q6cm48 , klula-q6cm49 , klula-q6cmt5 , klula-q6cn71 , klula-q6cnm1 , klula-q6cr74 , klula-q6cr90 , klula-q6crs0 , klula-q6crv8 , klula-q6crz9 , klula-q6cst8 , klula-q6csv8 , klula-q6ctp8 , klula-q6cu02 , klula-q6cu78 , klula-q6cu79 , klula-q6cuv3 , klula-q6cvd3 , klula-q6cw70 , klula-q6cw92 , klula-q6cwu7 , klula-q6cx84 , klula-q6cxa3 , klula-q6cy41 , yarli-apth1 , yarli-atg15 , yarli-BST1B , yarli-lip2 , yarli-LIP3 , yarli-LIP4 , yarli-LIP5 , yarli-LIP7 , yarli-LIP8 , yarli-lipa1 , yarli-ppme1 , yarli-q6bzp1 , yarli-q6bzv7 , yarli-q6c1f5 , yarli-q6c1f7 , yarli-q6c1r3 , yarli-q6c2z2 , yarli-q6c3h1 , yarli-q6c3i6 , yarli-q6c3l1 , yarli-q6c3u6 , yarli-q6c4h8 , yarli-q6c5j1 , yarli-q6c5m4 , yarli-q6c6m4 , yarli-q6c6p7 , yarli-q6c6v2 , yarli-q6c7h3 , yarli-q6c7i7 , yarli-q6c7j5 , yarli-q6c7y6 , yarli-q6c8m4 , yarli-q6c8q4 , yarli-q6c8u4 , yarli-q6c8y2 , yarli-q6c9r0 , yarli-q6c9r1 , yarli-q6c9u0 , yarli-q6c9v4 , yarli-q6c209 , yarli-q6c225 , yarli-q6c493 , yarli-q6c598 , yarli-q6c687 , yarli-q6c822 , yarli-q6cau6 , yarli-q6cax2 , yarli-q6caz1 , yarli-q6cb63 , yarli-q6cba7 , yarli-q6cbb1 , yarli-q6cbe6 , yarli-q6cby1 , yarli-q6ccr0 , yarli-q6cdg1 , yarli-q6cdi6 , yarli-q6cdv9 , yarli-q6ce37 , yarli-q6ceg0 , yarli-q6cep3 , yarli-q6cey5 , yarli-q6cf60 , yarli-q6cfp3 , yarli-q6cfx2 , yarli-q6cg13 , yarli-q6cg27 , yarli-q6cgj3 , yarli-q6chb8 , yarli-q6ci59 , yarli-q6c748 , canga-q6fpj0 , klula-q6cp11 , yarli-q6c4p0 , debha-q6btp5 , debha-kex1

Title : Different functions of fetal and adult AChR subtypes for the formation and maintenance of neuromuscular synapses revealed in epsilon-subunit-deficient mice - Schwarz_2000_Eur.J.Neurosci_12_3107
Author(s) : Schwarz H , Giese G , Muller H , Koenen M , Witzemann V
Ref : European Journal of Neuroscience , 12 :3107 , 2000
Abstract : Mice deficient in epsilon-subunits of the acetylcholine receptor (AChR) channel die prematurely due to severe AChR deficiency that leads to the progressive reduction in AChR density at the neuromuscular endplate [Witzemann, V., Schwarz, H., Koenen, M., Berberich, C., Villarroel, A., Wernig, A., Brenner, H.R. & Sakmann, B. (1996) Proc. Natl Acad. Sci. USA, 93, 13286-13291]. The mice may serve as a model for studying AChR-related myasthenic diseases. The postnatal development of the subsynaptic apparatus takes place in the absence of the adult type, epsilon-subunit-containing receptors which normally replace the fetal gamma-subunit-containing receptors. During later development the secondary folds of the postsynaptic membrane disappear concomitant with the decrease in AChR density, so that the flattened-out membrane with its remaining nicotinic receptors is in close proximity to the subsynaptic cytoplasmatic compartment and the subsynaptic myonuclei. The decrease in AChR concentration is correlated with a decrease of postsynaptic rapsyn, but has less effect on agrin, a neuronally released aggregating factor for AChRs. Thus, despite the presence of agrin at the synapse, AChR expression is not maintained at the level required to stabilize normal synaptic structure comprising secondary postsynaptic membrane folds. Collectively the results suggest that the postnatal switch from the global, activity-sensitive gamma-subunit gene transcription to the synapse-specific, activity-independent epsilon-subunit gene transcription is not required for the formation and differentiation of synapses but is essential for the maintenance of the highly organized structure of the neuromuscular endplate.
ESTHER : Schwarz_2000_Eur.J.Neurosci_12_3107
PubMedSearch : Schwarz_2000_Eur.J.Neurosci_12_3107
PubMedID: 10998094

Title : Organ selectivity of hexahydrosiladifenidol in blocking pre- and postjunctional muscarinic receptors studied in guinea-pig ileum and rat heart - Fuder_1985_Eur.J.Pharmacol_113_125
Author(s) : Fuder H , Kilbinger H , Muller H
Ref : European Journal of Pharmacology , 113 :125 , 1985
Abstract : Pre- and postjunctional pA2 values of the muscarinic antagonist hexahydrosiladifenidol were determined with guinea-pig ileum and rat heart. Hexahydrosiladifenidol did not discriminate between pre- and postjunctional receptors within the same organ but was more potent on the ileum (20-80 times) than on the heart. It is concluded that pre- and postjunctional muscarinic receptors in the heart may differ from those in the ileum.
ESTHER : Fuder_1985_Eur.J.Pharmacol_113_125
PubMedSearch : Fuder_1985_Eur.J.Pharmacol_113_125
PubMedID: 3840090