Anapoe20 (Tween20) and dodecyl maltoside (lauryl maltoside; DDM) were purchased from Anatrace (Maumee, OH). Docosahexaenoic acid (DHA) was purchased from Cayman Chemicals (Ann Arbor, MI). Cholesterol, deoxycholate (DOC), and retinoic acid (RA) were purchased from Sigma. Asolectin (soybean polar lipids) was reported by the supplier (Avanti Polar Lipids, Alabaster, AL) to contain 45.7% phosphatidylcholine, 22.1% phosphatidylethanolamine, 18.4% phosphatidylinositol, 6.9% phosphatidic acid, and 6.9% unspecified phospholipids and pigments as determined by HPLC/ELSD.
Dodecyl maltoside
Manufactured by Anatrace
Dodecyl maltoside (DM) is a non-ionic detergent commonly used in biochemical applications. It is a mild detergent that helps solubilize and stabilize membrane proteins. DM is often employed in the purification and functional studies of membrane-bound proteins.
Automatically generated - may contain errors
Lab products found in correlation
Deoxycholate, by Merck Group (1 mentions)
Docosahexaenoic acid dha, by Cayman Chemical (1 mentions)
Cholesterol, by Merck Group (1 mentions)
Retinoic acid, by Merck Group (1 mentions)
Asolectin, by Avanti Polar Lipids (1 mentions)
Deuterium oxide, by Cambridge Isotopes (1 mentions)
Sodium ascorbate, by Merck Group (1 mentions)
Valinomycin, by Merck Group (1 mentions)
Carbonyl cyanide 3 chlorophenylhydrazone, by Merck Group (1 mentions)
Phenol red, by Merck Group (1 mentions)
Sodium cholate, by Merck Group (1 mentions)
Crotalus atrox venom, by Merck Group (1 mentions)
Dioleoylphosphatidylcholine, by Avanti Polar Lipids (1 mentions)
Dioleoylphosphatidylethanolamine, by Avanti Polar Lipids (1 mentions)
Bovine cardiolipin, by Avanti Polar Lipids (1 mentions)
Bio beads sm 2, by Bio-Rad (1 mentions)
Horse heart cytochrome c, by Merck Group (1 mentions)
Potassium cyanide, by Merck Group (1 mentions)
Catalase, by Merck Group (1 mentions)
Potassium ferrocyanide, by Merck Group (1 mentions)
5 protocols using dodecyl maltoside
1
Lipid Composition Analysis Protocol
2
Lipid Hydroperoxide Synthesis and Purification
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Dodecyl maltoside was obtained from Anatrace. LTA4 methyl ester (BIOMOL) in tetrahydrofuran was saponified with 1 M LiOH (6%, v/v) for 48 h at 4°C. All other chemicals were obtained from common commercial sources. S-Hexyl GSH was synthesized as described in [16] .
3
Rhodopsin Preparation and Spin Labeling
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SDS (electrophoresis grade) was purchased from Bio-Rad (Hercules,
CA) and dodecyl maltoside (DM) from Anatrace (Maumee, OH). Deuterated
SDS and urea, deuterium oxide, [15N]-α-lysine, and
[15N]-α,ε-tryptophan were purchased from Cambridge
Isotope Laboratories (Cambridge, MA), and the methanethiosulfonate
spin label (MTSL) was from Toronto Research Chemicals (Toronto, ON).
Rhodopsin for NMR studies was purified from a tetracycline inducible
HEK 293S cell line stably transfected with the wild-type opsin gene,
as described previously.25 (link) All samples
were purified in 10 mM sodium phosphate buffer containing 0.05% DM.
Rhodopsin mutants for EPR studies (N151C, I154C, M155C, T108C, V204C,
and I205C) were obtained by site-directed mutagenesis according to
the established Stratagene protocol. Mutants were expressed by DEAE-Dextran
transient transfection of COS-1 cells and harvested after 60 h. Spin
labeling to introduce the nitroxide side chain designated R1 and purification
of each mutant were conducted on an immunoaffinity column as described
previously.38 (link)
CA) and dodecyl maltoside (DM) from Anatrace (Maumee, OH). Deuterated
SDS and urea, deuterium oxide, [15N]-α-lysine, and
[15N]-α,ε-tryptophan were purchased from Cambridge
Isotope Laboratories (Cambridge, MA), and the methanethiosulfonate
spin label (MTSL) was from Toronto Research Chemicals (Toronto, ON).
Rhodopsin for NMR studies was purified from a tetracycline inducible
HEK 293S cell line stably transfected with the wild-type opsin gene,
as described previously.25 (link) All samples
were purified in 10 mM sodium phosphate buffer containing 0.05% DM.
Rhodopsin mutants for EPR studies (N151C, I154C, M155C, T108C, V204C,
and I205C) were obtained by site-directed mutagenesis according to
the established Stratagene protocol. Mutants were expressed by DEAE-Dextran
transient transfection of COS-1 cells and harvested after 60 h. Spin
labeling to introduce the nitroxide side chain designated R1 and purification
of each mutant were conducted on an immunoaffinity column as described
previously.38 (link)
4
Reconstitution of Cytochrome c Oxidation
5
Isolation and Characterization of Cytochrome c Oxidase
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Potassium phosphate monobasic and dibasic, potassium hydroxide, potassium ferricyanide, potassium ferrocyanide, potassium sulfate, potassium cyanide, horse heart cytochrome c, superoxide dismutase (SOD), horseradish peroxidase type VI A, and catalase from bovine liver were purchased from Sigma-Aldrich, Triton X-100 (TX) was from Roche Diagnostics, dodecyl maltoside (DM) from Anatrace, Sepharose Q fast flow from Pharmacia Uppsala and hydrogen peroxide solution (~30%) was from Fluka.
Bovine heart cytochrome c oxidase was isolated from mitochondria following the modified method [86 (link)] into 10 mM Tris, pH 7.6, 50 mM K2SO4, and 0.1% TX. To change TX for DM detergent, the purified enzyme was diluted and reconcentrated using microfilters (YM 100, Millipore, cut-off 100 kDa) with the buffer containing 0.1% DM.
Isolated CcO was frozen in liquid nitrogen and stored at −80 °C. The concentration of CcO was determined from the UV-Vis absorption spectrum of the oxidized enzyme using an extinction coefficient ε (424 nm) = 156 mM−1cm−1 and ε (428 nm) = 169 mM−1cm−1 for the cyanide-ligated CcO (CcO.CN) [87 (link)].
Bovine heart cytochrome c oxidase was isolated from mitochondria following the modified method [86 (link)] into 10 mM Tris, pH 7.6, 50 mM K2SO4, and 0.1% TX. To change TX for DM detergent, the purified enzyme was diluted and reconcentrated using microfilters (YM 100, Millipore, cut-off 100 kDa) with the buffer containing 0.1% DM.
Isolated CcO was frozen in liquid nitrogen and stored at −80 °C. The concentration of CcO was determined from the UV-Vis absorption spectrum of the oxidized enzyme using an extinction coefficient ε (424 nm) = 156 mM−1cm−1 and ε (428 nm) = 169 mM−1cm−1 for the cyanide-ligated CcO (CcO.CN) [87 (link)].
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