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Literature summary for 3.4.24.27 extracted from

  • Hardre, H.; Kuhn, L.; Albrieux, C.; Jouhet, J.; Michaud, M.; Seigneurin-Berny, D.; Falconet, D.; Block, M.; Marechal, E.
    The selective biotin tagging and thermolysin proteolysis of chloroplast outer envelope proteins reveals information on protein topology and association into complexes (2014), Front. Plant Sci., 5, 203.
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
analysis selective biotin tagging and thermolysin proteolysis of chloroplast outer envelope proteins reveals information on protein topology and association into complexes. Development and evaluation of a method providing information at the surface of the outer envelope membrane, based on specific tagging with biotin or proteolysis using thermolysin, a non-membrane permeable protease. Envelope, thylakoid, and stroma proteins are separated by two-dimensional electrophoresis and analyzed by immunostaining and mass spectrometry, overview Bacillus thermoproteolyticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus thermoproteolyticus isolated intact chloroplast from Spinacia oleracea are treated with thermolysin, mass spectrometric analysis and two-dimensional analysis of shedded envelope proteins, including 28 kDa ribonucleoprotein, cytosolic HSP70/Com70, translocon Tic40-like protein, ClpC, HSP70, and hexokinase 1, overview ?
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Organism

Organism UniProt Comment Textmining
Bacillus thermoproteolyticus
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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 Bacillus thermoproteolyticus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information isolated intact chloroplast from Spinacia oleracea are treated with thermolysin, mass spectrometric analysis and two-dimensional analysis of shedded envelope proteins, including 28 kDa ribonucleoprotein, cytosolic HSP70/Com70, translocon Tic40-like protein, ClpC, HSP70, and hexokinase 1, overview Bacillus thermoproteolyticus ?
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General Information

General Information Comment Organism
additional information development and evaluation of a method providing information at the surface of the outer envelope membrane, based on specific tagging with biotin or proteolysis using thermolysin, a non-membrane permeable protease. Envelope, thylakoid, and stroma proteins are separated by two-dimensional electrophoresis and analyzed by immunostaining and mass spectrometry, overview Bacillus thermoproteolyticus