Preparative labeling of proteins with [35S]methionine

Browder, Leon W.; Wilkes, Jillian; Rodenhiser, David I.

doi:10.1016/0003-2697(92)90143-u

Cited by 12 publications

(4 citation statements)

References 4 publications

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“…These techniques of profiling translation, while powerful, do not address being able to visualize and quantify translation in intact cellular structures. A number of metabolic labeling techniques, inspired by earlier pioneering work using radioisotope‐labeled methionine , have allowed us to visualize where translation occurs in cells. These include techniques such as fluorescent noncanonical amino acid tagging (FUNCAT) , which uses a methionine analog, and puromyocin labeling to visualize newly synthesized proteins.…”

Section: Studying Local Translational Regulation: the Ever‐improving mentioning

confidence: 99%

Spatially and temporally regulating translation via mRNA‐binding proteins in cellular and neuronal function

2017

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Edited by Wilhelm JustCoordinated regulation of mRNA localization and local translation are essential steps in cellular asymmetry and function. It is increasingly evident that mRNA-binding proteins play critical functions in controlling the fate of mRNA, including when and where translation occurs. In this review, we discuss the robust and complex roles that mRNA-binding proteins play in the regulation of local translation that impact cellular function in vertebrates. First, we discuss the role of local translation in cellular polarity and possible links to vertebrate development and patterning. Next, we discuss the expanding role for local protein synthesis in neuronal development and function, with special focus on how a number of neurological diseases have given us insight into the importance of translational regulation. Finally, we discuss the everincreasing set of tools to study regulated translation and how these tools will be vital in pushing forward and addressing the outstanding questions in the field.

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Section: Studying Local Translational Regulation: the Ever‐improving mentioning

confidence: 99%

Spatially and temporally regulating translation via mRNA‐binding proteins in cellular and neuronal function

2017

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“…Proteins can be labeled with heavy variants of Met without risking isotope dilution into other amino acids using cell culture protocols that have been established since many years for 35 S-Met protein labeling (e.g., [22]). Only for post-translationally methylated proteins there is a transfer of the 13 C-methyl group from methionine via the activated methyl pathway (see below).…”

Section: G a L L E Y P R O O Fmentioning

confidence: 99%

Stable isotopic labeling in proteomics

et al. 2008

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Labeling of proteins and peptides with stable heavy isotopes (deuterium, carbon-13, nitrogen-15, and oxygen-18) is widely used in quantitative proteomics. These are either incorporated metabolically in cells and small organisms, or postmetabolically in proteins and peptides by chemical or enzymatic reactions. Only upon measurement with mass spectrometers holding sufficient resolution, light, and heavy labeled peptide ions or reporter peptide fragment ions segregate and their intensity values are subsequently used for quantification. Targeted use of these labels or mass tags further leads to specific monitoring of diverse aspects of dynamic proteomes. In this review article, commonly used isotope labeling strategies are described, both for quantitative differential protein profiling and for targeted analysis of protein modifications.

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“…Reaction of this protected amino acid with an excess of peptide 7 (using hydroxybenzomazole and dicyclohexylcarbodiimide for activation) gave the protected Org 5970-precursor S in radiochemical yields of 0,2 to 6,2 %. After deprotection with trifluoroacetic acid (in the presence of anisole and di-t-butyldisulphide) 35S-Org 5970 (2) was obtained. The product was purified by HPLC resulting in a product with a radiochemical purity of 2 95% (see Figure 5).…”

Section: Synthetic Approachesmentioning

confidence: 99%

Neuropeptides labelled with ³⁵S

Kaspersen

Nispen

Sperling

et al. 1993

Labelled Comp Radiopharmac

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Methionine and cysteine containing peptides can be labelled with 35S by coupling of 35S-cysteine or 35S-methionine with a large excess of suitably protected peptide precursors. This is illuslrated for [pGlu4, Cyt6]AVP-(4-9), P-endorphin-(5-17) and the ACTH-fragment-analogue Org 2766. Using HPLC as final purification the peptides are obtained in radiochemical yields of about 5% and radiochemical purities between 90-97%.However the specific activities obtained are much lower than the specific activities of the starting 35S-amino acids.

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Preparative labeling of proteins with [35S]methionine

Cited by 12 publications

References 4 publications

Spatially and temporally regulating translation via mRNA‐binding proteins in cellular and neuronal function

Spatially and temporally regulating translation via mRNA‐binding proteins in cellular and neuronal function

Stable isotopic labeling in proteomics

Neuropeptides labelled with ³⁵S

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Preparative labeling of proteins with [35S]methionine

Cited by 12 publications

References 4 publications

Spatially and temporally regulating translation via mRNA‐binding proteins in cellular and neuronal function

Spatially and temporally regulating translation via mRNA‐binding proteins in cellular and neuronal function

Stable isotopic labeling in proteomics

Neuropeptides labelled with 35S

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Neuropeptides labelled with ³⁵S