Determination of transglutaminase activity in plants
Autor: | Donatella Serafini-Fracassini, S. Del Duca, Giampiero Cai, Iris Aloisi, Philip L.R. Bonner |
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Přispěvatelé: | Del Duca, S., Ruben Alcazar, Antonio Tiburcio, Bonner, P.L.R., Aloisi, I., Serafini-Fracassini, D., Cai, G. |
Jazyk: | angličtina |
Rok vydání: | 2018 |
Předmět: |
0106 biological sciences
0301 basic medicine integumentary system biology Tissue transglutaminase Chemistry 01 natural sciences Polyamineâ protein interaction Actin filament binding assay Glutamyl-polyamines Glutamyl-polyamine 03 medical and health sciences 030104 developmental biology Transglutaminase activity Biochemistry Covalent bond Polyamineâprotein interaction biology.protein Microtubule binding/motility assay Genetics Transglutaminase assay Molecular Biology Cytoskeleton 010606 plant biology & botany |
Zdroj: | Methods in Molecular Biology ISBN: 9781493973972 |
Popis: | Transglutaminase (TGase:E.C. 2.3.2.13) catalyzes the acyl-transfer reaction between one or two primary amino groups of polyamines and protein-bound Gln residues giving rise to post-translational modifications. One increasing the positive charge on a proteins surface and the other results in the covalent crosslinking of proteins. Pioneering studies on TGase in plants started in the middle of the 1980âs but the methodology designed for use with animal extracts was not directly applicable to plant extracts. Here we describe radioactive and colorimetric methods adapted to study plant TGase, as well as protocols to analyze the involvement of TGase and polyamines in the functionality of cytoskeletal proteins. |
Databáze: | OpenAIRE |
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