[go: up one dir, main page]

Squier et al., 1987 - Google Patents

Localization of site-specific probes on the Ca-ATPase of sarcoplasmic reticulum using fluorescence energy transfer.

Squier et al., 1987

View HTML
Document ID
17960452062186677962
Author
Squier T
Bigelow D
de Ancos J
Inesi G
Publication year
Publication venue
Journal of Biological Chemistry

External Links

Snippet

Highly reactive sulfhydryls, previously labeled with an iodoacetamide spin label on the Ca- ATPase of sarcoplasmic reticulum, were labeled with the fluorescent probe, 5-(2-[iodoacetyl) amino) ethyl) aminonaphthalene-1-sulfonic acid (IAEDANS), without loss of enzymatic …
Continue reading at www.sciencedirect.com (HTML) (other versions)

Classifications

    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/53Immunoassay; Biospecific binding assay
    • G01N33/536Immunoassay; Biospecific binding assay with immune complex formed in liquid phase
    • G01N33/542Immunoassay; Biospecific binding assay with immune complex formed in liquid phase with steric inhibition or signal modification, e.g. fluorescent quenching
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N33/00Investigating or analysing materials by specific methods not covered by the preceding groups
    • G01N33/48Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
    • G01N33/50Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
    • G01N33/58Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving labelled substances
    • G01N33/582Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving labelled substances with fluorescent label
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N21/00Investigating or analysing materials by the use of optical means, i.e. using infra-red, visible or ultra-violet light
    • G01N21/17Systems in which incident light is modified in accordance with the properties of the material investigated
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N21/00Investigating or analysing materials by the use of optical means, i.e. using infra-red, visible or ultra-violet light
    • G01N21/62Systems in which the material investigated is excited whereby it emits light or causes a change in wavelength of the incident light
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N27/00Investigating or analysing materials by the use of electric, electro-chemical, or magnetic means
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2500/00Screening for compounds of potential therapeutic value
    • GPHYSICS
    • G01MEASURING; TESTING
    • G01NINVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N2333/00Assays involving biological materials from specific organisms or of a specific nature

Similar Documents

Publication Publication Date Title
Squier et al. Localization of site-specific probes on the Ca-ATPase of sarcoplasmic reticulum using fluorescence energy transfer.
Smith et al. Interaction of the adipocyte fatty acid-binding protein with the hormone-sensitive lipase: regulation by fatty acids and phosphorylation
Hendriks et al. Protonation/deprotonation reactions triggered by photoactivation of photoactive yellow protein from Ectothiorhodospira halophila
Uttamapinant et al. A fluorophore ligase for site-specific protein labeling inside living cells
Fanara et al. Quantitative analysis of nuclear localization signal (NLS)-importin α interaction through fluorescence depolarization: Evidence for auto-inhibitory regulation of NLS binding
Yamasaki et al. Interactive binding to the two principal ligand binding sites of human serum albumin: effect of the neutral-to-base transition
Horton et al. A substrate for deubiquitinating enzymes based on time-resolved fluorescence resonance energy transfer between terbium and yellow fluorescent protein
Riddle et al. Time-resolved fluorescence resonance energy transfer kinase assays using physiological protein substrates: Applications of terbium–fluorescein and terbium–green fluorescent protein fluorescence resonance energy transfer pairs
Li et al. Fluorescence detection techniques for protein kinase assay
Ojha et al. Imaging of fluorescence anisotropy during photoswitching provides a simple readout for protein self-association
Bigelow et al. Frequency-domain fluorescence spectroscopy resolves the location of maleimide-directed spectroscopic probes within the tertiary structure of the calcium ATPase of sarcoplasmic reticulum
Chen et al. Masking of a nuclear signal motif by monoubiquitination leads to mislocalization and degradation of the regulatory enzyme cytidylyltransferase
Choi et al. High-affinity free ubiquitin sensors for quantifying ubiquitin homeostasis and deubiquitination
Watanabe et al. Multicolor protein labeling in living cells using mutant β-lactamase-tag technology
Gursahani et al. Acidification reduces mitochondrial calcium uptake in rat cardiac mitochondria
Rakotoarison et al. Improving Split Reporters of Protein–Protein Interactions through Orthology-Based Protein Engineering
Yang et al. Simultaneous Measurement of SUMOylation using SNAP/CLIP‐Tag‐Mediated Translation at the Single‐Molecule Level
Gautier et al. Fluorogenic Protein‐Based Strategies for Detection, Actuation, and Sensing
Bhattacharya et al. Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes
Wang et al. A ratiometric fluorescent biosensor reveals dynamic regulation of long‐chain fatty acyl‐CoA esters metabolism
Kyrychenko et al. Joint refinement of FRET measurements using spectroscopic and computational tools
Chan et al. Rapid and Selective Labeling of Endogenous Transmembrane Proteins in Living Cells with a Difluorophenyl Ester Affinity‐Based Probe
US10302631B2 (en) Genetically encoded probe for quantification of pyruvate concentration and methods of using the same
Bigelow et al. Phosphorylation-dependent changes in the spatial relationship between Ca-ATPase polypeptide chains in sarcoplasmic reticulum membranes.
Rahman et al. Biochemical and structural characterization of analogs of MRE11 breast cancer-associated mutant F237C