Electrotransfer of proteins following polyacrylamide gel electrophoresis

Miribel, Laurent; Arnaúd, Philippe

doi:10.1016/0022-1759(88)90226-8

Cited by 23 publications

(3 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…They visualized SiaNAz-labeled molecules in extracted RNA samples using an RNA (Northern) blotting-like method 1 . This approach can pose several potential complications, such as the use of nitrocellulose membranes for RNA transfer which overall perform less efficiently in RNA detection than positively charged nylon membranes 16,17 . To overcome the limitations of RNA blotting, we developed a simpler approach that eliminated the need for RNA membrane transfer (see methods) and instead relied onlabelling SiaNAz-containing molecules with dibenzocyclooctyne-Cy5 (DBCO-Cy5) for direct fluorescent detection (Fig.…”

Section: Resultsmentioning

confidence: 99%

N-glycosylated molecules act as a co-precipitant in RNA purification

Kim,

Choi,

Janssen

et al. 2024

Preprint

View full text Add to dashboard Cite

A recent ground-breaking study suggested that small RNA from mammalian cells can undergo N-glycan modifications (termed glycoRNA). The discovery relied upon a metabolic glycan labeling strategy in combination with commonly used phase-separation-based RNA isolation. Following the reported procedure, we likewise identified an N-glycosylated species in the RNA fraction. However, our results suggest that the reported RNase sensitivity of the glycosylated species depends on the specific RNA purification method. This suggests the possibility of co-purifying unexpected RNase-insensitive N-glycoconjugates during glycoRNA isolation, hinting at the complex biochemical nature of glycoRNA. Our study underscores the need for further research to elucidate the structural and biochemical properties of glycoRNA.

show abstract

Section: Resultsmentioning

confidence: 99%

N-glycosylated molecules act as a co-precipitant in RNA purification

Kim,

Choi,

Janssen

et al. 2024

Preprint

View full text Add to dashboard Cite

show abstract

“…After electrophoresis, the protein was electroblotted onto a sheet of nitrocellulose (Millipore HAHY 00010) at 500 mA for 1 h [ 19 , 20 ]. The nitrocellulose was blocked by incubation with 5% (w/v) Marvel (dried skimmed milk) in PBS (phosphate buffered saline; 0.25 M NaCl, 0.0268 M KCl, 0.081 M Na 2 HPO 4 and 0.0146 M KH 2 PO 4 ) for 1 h, washed three times with PBST (PBS containing 0.1% (w/v) Tween 80; 10 min per wash).…”

Section: Methodsmentioning

confidence: 99%

Measurement of IgG Levels Can Serve as a Biomarker in Newly Diagnosed Diabetic Children

Haroun

El‐Sayed

2007

J. Clin. Biochem. Nutr.

View full text Add to dashboard Cite

Summary This study was undertaken to determine humoral immune response to the presence of anti-immunoglobulin antibodies in children with newly diagnosed type 1 diabetes mellitus, using as a target cow immunoglobulins, in an attempt to elucidate further complex immunopathogenetic interactions of the disease. Serum immunoglobulin G (IgG) concentrations were measured by ELISA in 30 children with type 1 diabetes mellitus and 30 healthy matched normal children. It was found that normal children had a mean IgG level of 7.41 mg/ml while diabetic individuals had a mean IgG level of 8.52 mg/ml (p<0.00004). On the contrary, the mean level of IgG in diabetic sera after purification from anti-cow immunoglobulins was determined to be 7.52 mg/ml. Therefore, there was no significant difference in IgG level in patients with type 1 diabetes mellitus after removal of anti-cow immunoglobulin antibodies compared to normal children (p<0.58). Visualization of IgG and immuno-precipitation confirm that anti-cow immunoglobulins antibodies, which were unrelated to antigen, were coprecipitated with the antigen-antibody complex. A circulating immunoglobulin reacting with other immunoglobulins is thus present in children with type 1 diabetes and may well play a part in the complex immuno-pathogenetic interactions.

show abstract

“…In addition, gels were incubated in 4-chloro-1-naphthol/H 2 O 2 (Serva, Merck) mainly to intensify minor haemoglobin components by their pseudoperoxidase activity. The staining solution consisted of 60 ml methanol and 340 ml PBS (pH 7·4) containing 120 mg 4-chloro-1-naphthol and 1 ml 30% H 2 O 2 (Miribel & Arnaud, 1988). Gels were also counterstained with Coomassie Brilliant Blue G-250 (Serva).…”

Section: Isoelectric Focusingmentioning

confidence: 99%

Population genetic analysis of the haemoglobins of the black‐chinned tilapia

Falk

Abban

Villwock

1999

Journal of Fish Biology

View full text Add to dashboard Cite

Three highly heterogeneous haemoglobin phenotypes, each composed of 22 different haemoglobin components, were identified among 17 West African populations of Sarotherodon melanotheron. Natural populations from (1) Senegal, (2) Ivory Coast/Ghana/Togo/Benin, and (3) Congo were distinguished. The heterogeneity and specificity of these respiratory pigments was based on genetic variations at the globin chain coding loci. In total, five different -chains and four different -chains were detected by acidic urea polyacrylamide gel electrophoresis (PAGE). Combinations of -chains were characteristic for populations in (1) Senegal, (2) Ivory Coast, (3) Ghana/Togo/Benin, and (4) Congo. Pronounced variations at the -globin chain cluster were found by acidic urea triton PAGE. Cladistic analyses of the globin chain characteristics confirmed the validity of the following taxonomic units previously ranked as sub-species: (1) populations from Ivory Coast, Ghana, Togo and Benin belong to the sub-species S. m. melanotheron; (2) populations from Senegal form genetically a separate cluster representing the sub-species S. m. heudelotii; (3) the Congo population, morphologically considered to represent the sub-species S. m. nigripinnis, forms another distinct unit; but there was no evidence of S. m. paludinosus within the samples from Senegal. 1999 The Fisheries Society of the British Isles

show abstract

Electrotransfer of proteins following polyacrylamide gel electrophoresis

Cited by 23 publications

References 20 publications

N-glycosylated molecules act as a co-precipitant in RNA purification

N-glycosylated molecules act as a co-precipitant in RNA purification

Measurement of IgG Levels Can Serve as a Biomarker in Newly Diagnosed Diabetic Children

Population genetic analysis of the haemoglobins of the black‐chinned tilapia

Contact Info

Product

Resources

About