Combining chymotrypsin/trypsin digestion to identify hydrophobic proteins from oil bodies

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F13%3A43896544" target="_blank" >RIV/60461373:22340/13:43896544 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22330/13:43896544

Výsledek na webu

<a href="http://dx.doi.org/10.1007/978-1-62703-631-3_14" target="_blank" >http://dx.doi.org/10.1007/978-1-62703-631-3_14</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/978-1-62703-631-3_14" target="_blank" >10.1007/978-1-62703-631-3_14</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Combining chymotrypsin/trypsin digestion to identify hydrophobic proteins from oil bodies

Popis výsledku v původním jazyce

Oil bodies, lipid-storage organelles, are stabilized by a number of specific proteins. These proteins are very hydrophobic, which complicates their identification by ?classical? proteomic protocols using trypsin digestion. Due to the lack of trypsin cleavage sites, the achievable protein coverage is limited or even insufficient for reliable protein identification. To identify such proteins and to enhance their coverage, we introduced a modified method comprising standard three-step procedure (SDS-PAGE,in-gel digestion, and LC-MS/MS analysis). In this method, chymotrypsin, single or in combination with trypsin, was used, which enabled to obtain proteolytic peptides from the hydrophobic regions and to identify new oil bodies? proteins. Our method can beeasily applied to identification of other hydrophobic proteins.

Název v anglickém jazyce

Combining chymotrypsin/trypsin digestion to identify hydrophobic proteins from oil bodies

Popis výsledku anglicky

Oil bodies, lipid-storage organelles, are stabilized by a number of specific proteins. These proteins are very hydrophobic, which complicates their identification by ?classical? proteomic protocols using trypsin digestion. Due to the lack of trypsin cleavage sites, the achievable protein coverage is limited or even insufficient for reliable protein identification. To identify such proteins and to enhance their coverage, we introduced a modified method comprising standard three-step procedure (SDS-PAGE,in-gel digestion, and LC-MS/MS analysis). In this method, chymotrypsin, single or in combination with trypsin, was used, which enabled to obtain proteolytic peptides from the hydrophobic regions and to identify new oil bodies? proteins. Our method can beeasily applied to identification of other hydrophobic proteins.

Druh

C - Kapitola v odborné knize

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název knihy nebo sborníku

Plant Proteomics, Methods and Protocols

ISBN

978-1-62703-630-6

Počet stran výsledku

14

Strana od-do

185-198

Počet stran knihy

786

Název nakladatele

Humana press

Místo vydání

New York

Kód UT WoS kapitoly

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