Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels

Blum, Helmut; Beier, Hildburg; Groß, H.

doi:10.1002/elps.1150080203

Cited by 3,897 publications

(2,084 citation statements)

References 28 publications

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“…Both the high and low molecular mass standards were from Pharmacia. Proteins were visualized by staining with either Coomassie Brilliant blue R-250 (Fluka, Buchs Switzerland) or silver [22]. Iron-containing proteins could also be visualized by the method of Kuo and Fridovich [23] either alone or in combination with Coomassie staining.…”

Section: Methodsmentioning

confidence: 99%

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Carrano¹,

Böhnke²,

Matzanke³

1996

FEBS Letters

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Two distinct ferritin like iron containing proteins have been identified and isolated from the fungus Absidia spinosa; one from the spores and another from the mycelia. The mycelial protein has been purified and consists of two subunits of approx. 20 kDa. The N-terminal sequences of both subunits have been determined. The holoprotein as isolated contains approx. 750 iron atoms/molecule and exhibits a beme-like UV-Vis spectrum. Based on the beme spectrum and the high degree of sequence homology found, it has been established that the mycelial protein is a bacterioferritin. This is the first example demonstrating the presence of a bacterioferritin in a eukaryotic organism.

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Section: Methodsmentioning

confidence: 99%

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Carrano¹,

Böhnke²,

Matzanke³

1996

FEBS Letters

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“…Quantified proteins (170 μg) were mixed in sample buffer and then loaded onto IEF gel (18 cm tube gel) (O'Farrell, 1975). In the second dimension, proteins were separated in 12% SDSpolyacrylamide gels and visualized by silver staining with no glutaraldehyde (Blum et al, 1987). Gel images were scanned using a GS-800 Imaging Densitometer (Bio-Rad) and analyzed with the software PDQuest version 7.2.0 (Bio-Rad).…”

Section: -De Analyses and Maldi-tof Msmentioning

confidence: 99%

Identification and Molecular Properties of SUMO-Binding Proteins in Arabidopsis

Park

Choi

Park

et al. 2011

Molecules and Cells

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Reversible conjugation of the small ubiquitin modifier (SUMO) peptide to proteins (SUMOylation) plays important roles in cellular processes in animals and yeasts. However, little is known about plant SUMO targets. To identify SUMO substrates in Arabidopsis and to probe for biological functions of SUMO proteins, we constructed 6xHis-3xFLAG fused AtSUMO1 (HFAtSUMO1) controlled by the CaMV35S promoter for transformation into Arabidopsis Col-0. After heat treatment, an increased sumoylation pattern was detected in the transgenic plants. SUMO1-modified proteins were selected after two-dimensional gel electrophoresis (2-DE) image analysis and identified using matrix-assisted laser-desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). We identified 27 proteins involved in a variety of processes such as nucleic acid metabolism, signaling, metabolism, and including proteins of unknown functions. Binding and sumoylation patterns were confirmed independently. Surprisingly, MCM3 (At5G46280), a DNA replication licensing factor, only interacted with and became sumoylated by AtSUMO1, but not by SUMO1ΔGG or AtSUMO3. The results suggest specific interactions between sumoylation targets and particular sumoylation enzymes.

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“…SDS-PAGE of clam cadmium-binding proteins purified by ion-exchange chromatography (CdMT-1; CdMT-2; CdMT-3) and MT-1 from rabbit liver (Sigma). Stained by the silver-stain method as described in Blum et al (1987). Lane-1, CdMT-1; Lane-2, CdMT-2; Lane-3, CdMT-3; Lane-4, MT-1 from rabbit liver (Sigma).…”

Section: Discussionmentioning

confidence: 99%

“…Stacking gels were 0.1% SDS, 5% polyacrylamide, and separating gels were 0.1% SDS and 17.5% polyacrylamide. Gels were stained by the Coomassie Blue G-250/H3PO4 protein staining method (Mitra et al, 1994) and by the silver-stain method (Blum et al, 1987).…”

Section: Metallothionein Purificationmentioning

confidence: 99%

Isolation and characterisation of metallothionein from the clam Ruditapes decussatus

2003

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Metallothioneins (MT) were obtained after purification from metal-exposed clams (Ruditapes decussatus ) using gelpermeation and ion-exchange chromatography. Four cadmium Á/metallothioneins (CdMTs) were resolved by ionexchange chromatography and they all had similar molecular weights, high cadmium content and an absorption spectra indicative of the presence of characteristic Cd Ã/S aggregates. The NH 2 -terminal sequence suggests the presence of at least two class I clam MT isoforms. For the other two putative clam CdMTs isolated, the results of the amino acid determination were inconclusive. One was slightly contaminated and the other one had a blocked NH 2 -terminal. These clam metalothioneins contain glycine, which seems to be a common feature of molluscan MT family and exhibited more similarity to oysters than to mussels. Further investigation on the inducibility of these isoforms will be necessary if clams are to be used as biomarkers of metal exposure. #

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Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels

Cited by 3,897 publications

References 28 publications

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Fungal ferritins: The ferritin from mycelia of Absidia spinosa is a bacterioferritin

Identification and Molecular Properties of SUMO-Binding Proteins in Arabidopsis

Isolation and characterisation of metallothionein from the clam Ruditapes decussatus

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