Physical and Structural Properties of Caleosin, A Protein Probably Involved in the Mechanisms of Lipid Bodies Maturation.
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F05%3A00015603" target="_blank" >RIV/60461373:22330/05:00015603 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Alternative languages
Result language
angličtina
Original language name
Physical and Structural Properties of Caleosin, A Protein Probably Involved in the Mechanisms of Lipid Bodies Maturation.
Original language description
Plants store energy as polysaccharides or lipids. Lipids are stored in intracellularoil particles called oil or lipid bodies, which can be found in all types of cells, but mainlyin seeds. Lipid bodies are made up of a core containing mainly neutral lipids. The coreis surrounded by a single monolayer of phospholipids embedded with structural proteins(oleosins). The function of oleosins is to maintain oil bodies in small stable droplets.Next to the oleosins the phospholipids monolayer contains also smallamount ofcaleosin. Caleosin structure is oleosin-like but on the other hand unique thanks to thepresence of calcium binding site.The mechanisms of lipid biosynthesis in plants is well known. However not somuch is known about the process of formation andmaturation of lipid bodies. Lipidbodies are believed to arise from specific microdomains of the endoplasmic reticulummembrane that contain the full complement of TAG-biosynthesis enzymes. The smallnascent lipid bodies undergo a series of
Czech name
Fysikální a strukturní vlastnosti caleosinu, proteinu pravděpodobně se účastnícího v mechanismu zrání lipidových tělísek.
Czech description
Fysikální a strukturní vlastnosti caleosinu, proteinu pravděpodobně se účastnícího v mechanismu zrání lipidových tělísek.
Classification
Type
O - Miscellaneous
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GA204%2F02%2F0843" target="_blank" >GA204/02/0843: Complex cold adaptation study of enzymes on molecular level and their application in biotechnology</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2005
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů