PUBLICACIÓN

The effect of a monoclonal antibody on specific steps of the reaction sequence of the (Ca2+-Mg2+)-ATPase from sarcoplasmic reticulum

ACCEDER A LA PUBLICACIÓN: Scopus

MATA, AM, COLYER, J, MICHELANGELI, F, LEE, AG, EAST, JM

1991 Biochemical Society Transactions

CITAS

0

DOI

10.1042/bst019205s

EID

2-s2.0-0025804517

ISSN

0300-5127

BIBTEX

@article{RID:0827140741255-50, title = {THE EFFECT OF A MONOCLONAL-ANTIBODY ON SPECIFIC STEPS OF THE REACTION SEQUENCE OF THE (CA2+-MG2+)-ATPASE FROM SARCOPLASMIC-RETICULUM}, journal = {Biochemical Society Transactions}, year = {1991}, author = {MATA, AM and COLYER, J and MICHELANGELI, F and LEE, AG and EAST, JM}, volume = {19}, number = {2}, pages = {S205} }

AUTORES DE LA UEX

Ana María Mata Durán

OTRAS PUBLICACIONES DE INTERÉS

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Effect Of Spermine On The Activity Of Synaptosomal Plasma Membrane Ca2+-Atpase Reconstituted In Neutral Or Acidic Phospholipids
Erratum: Effect Of Spermine On The Activity Of Synaptosomal Plasma Membrane Ca2+-Atpase Reconstituted In Neutral Or Acidic Phospholipids (Biochimica Et Biophysica Acta (2003) 1611 (197-203))
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Evidence That An Ant1-Serca1 Monoclonal Antibody Recognizes The Serca2b Calcium Pump In Pig Brain
Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain
Correction: Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain (Biochemical Journal (1996) 315 (183-187))
Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain
Correction: Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain (Biochemical Journal (1996) 315 (183-187))
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Correction: Purification Of The Synaptosomal Plasma Membrane (Ca2+ + Mg2+)-Atpase From Pig Brain (Biochemical Journal (1996) 315 (183-187))
The Modulation Of Ca2+ Binding To Sarcoplasmic Reticulum Atpase By Atp Analogues Is Ph-Dependent
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The Modulation Of Ca2+ Binding To Sarcoplasmic Reticulum Atpase By Atp Analogues Is Ph-Dependent
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Evidence For The Lumenal Location Of The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum
Identification Of Two Types Of Ca2+ Transport Atpases In Pig Brain By Specific Antibodies
Evidence For The Lumenal Location Of The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum
Reactivity Of Lysyl Residues On The (Ca2+-Mg2+)-Atpase To 7-Amino-4-Methylcoumarin-3-Acetic Acid Succinimidyl Ester
Evidence For The Lumenal Location Of The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum
Reactivity Of Lysyl Residues On The (Ca2+-Mg2+)-Atpase To 7-Amino-4-Methylcoumarin-3-Acetic Acid Succinimidyl Ester
Labeling The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum At Glu-439 With 5-(Bromomethyl)fluorescein
Reactivity Of Lysyl Residues On The (Ca2+-Mg2+)-Atpase To 7-Amino-4-Methylcoumarin-3-Acetic Acid Succinimidyl Ester
Labeling The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum At Glu-439 With 5-(Bromomethyl)fluorescein
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Localization Of Cys-344 On The (Ca2+ -Mg2+)-Atpase Of Sarcoplasmic Reticulum Using Resonance Energy Transfer
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Localization Of Cys-344 On The (Ca2+ -Mg2+)-Atpase Of Sarcoplasmic Reticulum Using Resonance Energy Transfer
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Definition Of Surface-Exposed And Trans-Membranous Regions Of The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum Using Anti-Peptide Antibodies
Studies Of The Structure And Function Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Immunological Approaches
An Examination Of The Transmembranous Organisation Of The Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Antipeptide Antibodies
Studies Of The Structure And Function Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Immunological Approaches
An Examination Of The Transmembranous Organisation Of The Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Antipeptide Antibodies
Definition Of An Epitope At The Nucleotide Binding Site Of The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum By Fluorescein Labelling
An Examination Of The Transmembranous Organisation Of The Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase Using Antipeptide Antibodies
Definition Of An Epitope At The Nucleotide Binding Site Of The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum By Fluorescein Labelling
Chemical Crosslinking And Enzyme Kinetics Provide No Evidence For A Regulatory Role For The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum In Calcium Transport
Definition Of An Epitope At The Nucleotide Binding Site Of The (Ca2+-Mg2+)-Atpase Of Sarcoplasmic Reticulum By Fluorescein Labelling
Chemical Crosslinking And Enzyme Kinetics Provide No Evidence For A Regulatory Role For The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum In Calcium Transport
Mapping Epitopes On The (Ca2+mg2+)-Atpase Of Sarcoplasmic Reticulum Using Fusion Proteins
Chemical Crosslinking And Enzyme Kinetics Provide No Evidence For A Regulatory Role For The 53 Kda Glycoprotein Of Sarcoplasmic Reticulum In Calcium Transport
Mapping Epitopes On The (Ca2+mg2+)-Atpase Of Sarcoplasmic Reticulum Using Fusion Proteins
The Effect Of A Monoclonal Antibody On Specific Steps Of The Reaction Sequence Of The (Ca2+-Mg2+)-Atpase From Sarcoplasmic Reticulum
Mapping Epitopes On The (Ca2+mg2+)-Atpase Of Sarcoplasmic Reticulum Using Fusion Proteins
The Effect Of A Monoclonal Antibody On Specific Steps Of The Reaction Sequence Of The (Ca2+-Mg2+)-Atpase From Sarcoplasmic Reticulum
Effect Of The Detergent C12e8 On The Binding Of Monoclonal Antibodies To The (Ca2+-Mg2+)-Atpase Of Rabbit Skeletal Sarcoplasmic Reticulum
The Effect Of A Monoclonal Antibody On Specific Steps Of The Reaction Sequence Of The (Ca2+-Mg2+)-Atpase From Sarcoplasmic Reticulum
Effect Of The Detergent C12e8 On The Binding Of Monoclonal Antibodies To The (Ca2+-Mg2+)-Atpase Of Rabbit Skeletal Sarcoplasmic Reticulum
Distribution Of Two Distinct Ca2+ -Atpase-Like Proteins And Their Relationships To The Agonist-Sensitive Calcium Store In Adrenal Chromaffin Cells
Effect Of The Detergent C12e8 On The Binding Of Monoclonal Antibodies To The (Ca2+-Mg2+)-Atpase Of Rabbit Skeletal Sarcoplasmic Reticulum
Distribution Of Two Distinct Ca2+ -Atpase-Like Proteins And Their Relationships To The Agonist-Sensitive Calcium Store In Adrenal Chromaffin Cells
Effects Of Atpase Activity Of Monoclonal Antibodies Raised Against (Ca2+ + Mg2+)-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum And Their Correlation With Epitope Location
Distribution Of Two Distinct Ca2+ -Atpase-Like Proteins And Their Relationships To The Agonist-Sensitive Calcium Store In Adrenal Chromaffin Cells
Effects Of Atpase Activity Of Monoclonal Antibodies Raised Against (Ca2+ + Mg2+)-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum And Their Correlation With Epitope Location
Probing The Nucleotide-Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase With Anti-Fluorescein Antibodies
Effects Of Atpase Activity Of Monoclonal Antibodies Raised Against (Ca2+ + Mg2+)-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum And Their Correlation With Epitope Location
Probing The Nucleotide-Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase With Anti-Fluorescein Antibodies
Evidence For The Cytoplasmic Location Of The N- And C-Terminal Segments Of Sarcoplasmic Reticulum (Ca2+mg2+)-Atpase
Probing The Nucleotide-Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2+)-Atpase With Anti-Fluorescein Antibodies
Evidence For The Cytoplasmic Location Of The N- And C-Terminal Segments Of Sarcoplasmic Reticulum (Ca2+mg2+)-Atpase
Probing The Nucleotide Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2)-Atpase With Anti-Fluorescein Antibodies
Evidence For The Cytoplasmic Location Of The N- And C-Terminal Segments Of Sarcoplasmic Reticulum (Ca2+mg2+)-Atpase
Probing The Nucleotide Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2)-Atpase With Anti-Fluorescein Antibodies
Use Of Antibodies To Detect Chemically Cross-Linked Products From Sarcoplasmic Reticulum
Probing The Nucleotide Binding Site Of Sarcoplasmic Reticulum (Ca2+-Mg2)-Atpase With Anti-Fluorescein Antibodies
Use Of Antibodies To Detect Chemically Cross-Linked Products From Sarcoplasmic Reticulum
Effect Of Monoclonal Antibodies Raised Against Ca2+,mg2+-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum On Atpase Activity And Its Correlation With Epitope Location
Use Of Antibodies To Detect Chemically Cross-Linked Products From Sarcoplasmic Reticulum
Effect Of Monoclonal Antibodies Raised Against Ca2+,mg2+-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum On Atpase Activity And Its Correlation With Epitope Location
The Position Of The Atp Binding Site On The (Ca2+ + Mg2+)-Atpase
Effect Of Monoclonal Antibodies Raised Against Ca2+,mg2+-Atpase From Rabbit Skeletal Muscle Sarcoplasmic Reticulum On Atpase Activity And Its Correlation With Epitope Location
The Position Of The Atp Binding Site On The (Ca2+ + Mg2+)-Atpase
Dependence Of The Fluorescence Of Fluorescein Labelled (Ca2+, Mg2+)-Atpase Upon The Lipid To Protein Ratio In Sarcoplasmic Reticulum Reconstituted Systems
The Position Of The Atp Binding Site On The (Ca2+ + Mg2+)-Atpase
Dependence Of The Fluorescence Of Fluorescein Labelled (Ca2+, Mg2+)-Atpase Upon The Lipid To Protein Ratio In Sarcoplasmic Reticulum Reconstituted Systems
Redox Interconversion Of Escherichia Coli Glutathione Reductase. A Study With Permeabilized And Intact Cells
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Redox Interconversion Of Escherichia Coli Glutathione Reductase. A Study With Permeabilized And Intact Cells
Redox Interconversion Of Glutathione Reductase From Escherichia Coli. A Study With Pure Enzyme And Cell-Free Extracts
Redox Interconversion Of Escherichia Coli Glutathione Reductase. A Study With Permeabilized And Intact Cells
Redox Interconversion Of Glutathione Reductase From Escherichia Coli. A Study With Pure Enzyme And Cell-Free Extracts
The Redox Interconversion Mechanism Of Saccahromyces Cerevisiae Glutathione Reductase
Redox Interconversion Of Glutathione Reductase From Escherichia Coli. A Study With Pure Enzyme And Cell-Free Extracts
The Redox Interconversion Mechanism Of Saccahromyces Cerevisiae Glutathione Reductase
Purification By Affinity Chromatography Of Glutathione Reductase (Ec 1.6.4.2) From Escherichia Coli And Characterization Of Such Enzyme
The Redox Interconversion Mechanism Of Saccahromyces Cerevisiae Glutathione Reductase
Purification By Affinity Chromatography Of Glutathione Reductase (Ec 1.6.4.2) From Escherichia Coli And Characterization Of Such Enzyme
Reversible Inactivation Of Saccharomyces Cerevisiae Glutathione Reductase Under Reducing Conditions
Purification By Affinity Chromatography Of Glutathione Reductase (Ec 1.6.4.2) From Escherichia Coli And Characterization Of Such Enzyme
Reversible Inactivation Of Saccharomyces Cerevisiae Glutathione Reductase Under Reducing Conditions
Neurotoxic Amyloid Β‐peptide And Tau Produce Cytokine‐like Effects On Pmca In Glioblastoma Cell Lines, Enhancing Its Activity And Isoforms Expression
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