Quantitative Plant Proteomics Using Hydroponic Isotope Labeling of Entire Plants (HILEP). / Bindschedler, Laurence ; Cramer, Rainer.

Sample Preparation for Biological Mass Spectrometry. . Springer, 2011. p. 363-380.

Research output: Chapter in Book/Report/Conference proceedingChapter

Published

Standard

Quantitative Plant Proteomics Using Hydroponic Isotope Labeling of Entire Plants (HILEP). / Bindschedler, Laurence ; Cramer, Rainer.

Sample Preparation for Biological Mass Spectrometry. . Springer, 2011. p. 363-380.

Research output: Chapter in Book/Report/Conference proceedingChapter

Harvard

Bindschedler, L & Cramer, R 2011, Quantitative Plant Proteomics Using Hydroponic Isotope Labeling of Entire Plants (HILEP). in Sample Preparation for Biological Mass Spectrometry. . Springer, pp. 363-380. https://doi.org/10.1007/978-94-007-0828-0_19

APA

Bindschedler, L., & Cramer, R. (2011). Quantitative Plant Proteomics Using Hydroponic Isotope Labeling of Entire Plants (HILEP). In Sample Preparation for Biological Mass Spectrometry. (pp. 363-380). Springer. https://doi.org/10.1007/978-94-007-0828-0_19

Vancouver

Bindschedler L, Cramer R. Quantitative Plant Proteomics Using Hydroponic Isotope Labeling of Entire Plants (HILEP). In Sample Preparation for Biological Mass Spectrometry. . Springer. 2011. p. 363-380 https://doi.org/10.1007/978-94-007-0828-0_19

Author

Bindschedler, Laurence ; Cramer, Rainer. / Quantitative Plant Proteomics Using Hydroponic Isotope Labeling of Entire Plants (HILEP). Sample Preparation for Biological Mass Spectrometry. . Springer, 2011. pp. 363-380

BibTeX

@inbook{77db92d6031c42a69e6493e064b4933b,
title = "Quantitative Plant Proteomics Using Hydroponic Isotope Labeling of Entire Plants (HILEP).",
abstract = "Hydroponic cultivation is a soil-free technique commonly used in agriculture where plants are grown in a highly controlled environment leading to high crop yields. Hydroponic Isotope Labeling of Entire Plants (HILEP) is the most cost-effective isotope labeling method for quantitative plant proteomics, enabling the metabolic labeling of whole and mature plants with a stable isotope such as 15N. Employing inorganic 15N-containing salts as the sole nitrogen source, healthy plants can be easily grown and labeled in hydroponic solutions. Close to 100% 15N-labeling of proteins can be achieved using HILEP. Moreover, hydroponic cultivation allows tight control of growth conditions. Plants grown in 14N- and 15N-hydroponic media are typically pooled straight after harvest, eliminating any bias due to subsequent sample preparation and analysis. The pooled 14N-/15N-protein extracts can be fractionated in any convenient way and digested with trypsin (or any other enzyme of choice). Peptides can then be analyzed by techniques such as liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS). Following protein identification, the spectra of 14N/15N-peptide pairs are typically compared and relative protein amounts are calculated from the 14N/15N-ion signal ratios. An increasing number of bioinformatics tools are now available for determining these ratios in a convenient way. ",
author = "Laurence Bindschedler and Rainer Cramer",
year = "2011",
doi = "10.1007/978-94-007-0828-0_19",
language = "English",
pages = "363--380",
booktitle = "Sample Preparation for Biological Mass Spectrometry.",
publisher = "Springer",

}

RIS

TY - CHAP

T1 - Quantitative Plant Proteomics Using Hydroponic Isotope Labeling of Entire Plants (HILEP).

AU - Bindschedler, Laurence

AU - Cramer, Rainer

PY - 2011

Y1 - 2011

N2 - Hydroponic cultivation is a soil-free technique commonly used in agriculture where plants are grown in a highly controlled environment leading to high crop yields. Hydroponic Isotope Labeling of Entire Plants (HILEP) is the most cost-effective isotope labeling method for quantitative plant proteomics, enabling the metabolic labeling of whole and mature plants with a stable isotope such as 15N. Employing inorganic 15N-containing salts as the sole nitrogen source, healthy plants can be easily grown and labeled in hydroponic solutions. Close to 100% 15N-labeling of proteins can be achieved using HILEP. Moreover, hydroponic cultivation allows tight control of growth conditions. Plants grown in 14N- and 15N-hydroponic media are typically pooled straight after harvest, eliminating any bias due to subsequent sample preparation and analysis. The pooled 14N-/15N-protein extracts can be fractionated in any convenient way and digested with trypsin (or any other enzyme of choice). Peptides can then be analyzed by techniques such as liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS). Following protein identification, the spectra of 14N/15N-peptide pairs are typically compared and relative protein amounts are calculated from the 14N/15N-ion signal ratios. An increasing number of bioinformatics tools are now available for determining these ratios in a convenient way.

AB - Hydroponic cultivation is a soil-free technique commonly used in agriculture where plants are grown in a highly controlled environment leading to high crop yields. Hydroponic Isotope Labeling of Entire Plants (HILEP) is the most cost-effective isotope labeling method for quantitative plant proteomics, enabling the metabolic labeling of whole and mature plants with a stable isotope such as 15N. Employing inorganic 15N-containing salts as the sole nitrogen source, healthy plants can be easily grown and labeled in hydroponic solutions. Close to 100% 15N-labeling of proteins can be achieved using HILEP. Moreover, hydroponic cultivation allows tight control of growth conditions. Plants grown in 14N- and 15N-hydroponic media are typically pooled straight after harvest, eliminating any bias due to subsequent sample preparation and analysis. The pooled 14N-/15N-protein extracts can be fractionated in any convenient way and digested with trypsin (or any other enzyme of choice). Peptides can then be analyzed by techniques such as liquid chromatography electrospray ionization tandem mass spectrometry (LC-ESI-MS/MS). Following protein identification, the spectra of 14N/15N-peptide pairs are typically compared and relative protein amounts are calculated from the 14N/15N-ion signal ratios. An increasing number of bioinformatics tools are now available for determining these ratios in a convenient way.

U2 - 10.1007/978-94-007-0828-0_19

DO - 10.1007/978-94-007-0828-0_19

M3 - Chapter

SP - 363

EP - 380

BT - Sample Preparation for Biological Mass Spectrometry.

PB - Springer

ER -