A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels

Oakley, Berl R; Kirsch, Donald R.; Morris, Nicholas P.

doi:10.1016/0003-2697(80)90470-4

Cited by 3,201 publications

(1,132 citation statements)

References 4 publications

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“…These standards appear along the basic edge of each gel. The gels were either silver [24] or Coomassie blue stained. Gels were dried between cellophane paper.…”

Section: Electrophoresismentioning

confidence: 99%

Proteomic changes in rat thyroarytenoid muscle induced by botulinum neurotoxin injection

et al. 2008

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Botulinum neurotoxin (BoNT) injection into the thyroarytenoid (TA) muscle is a commonly performed medical intervention for adductor spasmodic dysphonia. The mechanism of action of BoNT at the neuromuscular junction is well understood, however, aside from reports focused on myosin heavy chain isoform abundance, there is a paucity of data addressing the effects of therapeutic BoNT injection on the TA muscle proteome. In this study, 12 adult Sprague Dawley rats underwent unilateral TA muscle BoNT serotype A injection followed by tissue harvest at 72 hrs, 7 days, 14 days, and 56 days post-injection. Three additional rats were reserved as controls. Proteomic analysis was performed using 2D SDS-PAGE followed by MALDI-MS. Vocal fold movement was significantly reduced by 72 hrs, with complete return of function by 56 days. Twenty-five protein spots demonstrated significant protein abundance changes following BoNT injection, and were associated with alterations in energy metabolism, muscle contractile function, cellular stress response, transcription, translation, and cell proliferation. A number of protein abundance changes persisted beyond the return of gross physiologic TA function. These findings represent the first report of BoNT induced changes in any skeletal muscle proteome, and reinforce the utility of applying proteomic tools to the study of system-wide biological processes in normal and perturbed TA muscle function.

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“…These standards appear along the basic edge of each gel. The gels were either silver [24] or Coomassie blue stained. Gels were dried between cellophane paper.…”

Section: Electrophoresismentioning

confidence: 99%

Proteomic changes in rat thyroarytenoid muscle induced by botulinum neurotoxin injection

et al. 2008

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“…Silver staining with diamine or nitrate was carried out according to the methods [16][17][18][19][20]. The SYPRO Ruby staining procedure is described in Section 2.2.…”

Section: -D Electrophoresismentioning

confidence: 99%

A fluorescent natural product for ultra sensitive detection of proteins in one‐dimensional and two‐dimensional gel electrophoresis

et al. 2003

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Lightning Fast is a sensitive fluorescence-based stain for detecting proteins in onedimensional and two-dimensional polyacrylamide electrophoresis gels. It contains the fluorophore epicocconone from the fungus Epicoccum nigrum that interacts noncovalently with sodium dodecyl sulfate and protein. Stained proteins can be excited optimally by near-ultraviolet light of about 395 nm or with visible light of about 520 nm. The stain can be excited using a range of sources used in image analysis systems including UVA (ca. 365 nm) and UVB (ca. 302 nm) transilluminators; Xenon-arc lamps; 488 nm and 457 nm Argon-ion lasers; 473 nm and 532 nm neodymium: yttrium aluminum garnet (Nd:YAG) solid-state lasers; 543 nm helium-neon lasers, and emerging violet, blue and green diode lasers. Maximum fluorescence emission of the dye is at approximately 610 nm. The limit of detection in one-dimensional gels stained with Lightning Fast protein gel stain is less than 100 pg of protein, rivaling the current limits of matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-MS). Lightning Fast was found to be considerably more sensitive than SYPRO Ruby, SYPRO Orange, silver and Coomassie Brilliant Blue G-250 in matched experiments. Staining takes as little as 3.5 h and stained proteins displayed quantitative linearity over more than four orders of magnitude, thereby allowing visualization of entire proteomes. Lightning Fast protein gel staining is compatible with subsequent peptide mass fingerprinting using MALDI-MS and Edman-based sequencing chemistry.

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“…The gels were stained for protein with Coomassie Brilliant Blue or by the silver staining procedure of Oakley et al (21). Nondenaturing gel electrophoresis on 0.3% agarose-2.5% acrylamide gels was performed as described by Liu et al (22).…”

Section: Methodsmentioning

confidence: 99%

A molecular defect of spectrin in a subset of patients with hereditary elliptocytosis. Alterations in the alpha-subunit domain involved in spectrin self-association.

Lawler¹,

Liu²,

Palek³

et al. 1984

J. Clin. Invest.

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A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels

Cited by 3,201 publications

References 4 publications

Proteomic changes in rat thyroarytenoid muscle induced by botulinum neurotoxin injection

Proteomic changes in rat thyroarytenoid muscle induced by botulinum neurotoxin injection

A fluorescent natural product for ultra sensitive detection of proteins in one‐dimensional and two‐dimensional gel electrophoresis

A molecular defect of spectrin in a subset of patients with hereditary elliptocytosis. Alterations in the alpha-subunit domain involved in spectrin self-association.

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