Purification of a tonoplast polypeptide with sucrose transport properties

Autor:	Andrew Maretzki, Hans Peter Getz, Margaret Thom
Rok vydání:	1992
Předmět:	Liposome Chromatography Sucrose Physiology medicine.drug_class Chemistry Ion chromatography Size-exclusion chromatography Cell Biology Plant Science General Medicine Vacuole Carbohydrate Sucrose transport Monoclonal antibody chemistry.chemical_compound Biochemistry Genetics medicine
Zdroj:	Physiologia Plantarum. 86:104-114
ISSN:	1399-3054 0031-9317
DOI:	10.1111/j.1399-3054.1992.tb01318.x
Popis:	Sucrose uptake into vacuoles of sugarcane parenchyma cells is mediated by a transporter. A polypeptide fitting that description has been partially purified from solubilized tonoplast by gel filtration and ion exchange chromatography. Purification of the relevant polypeptide was followed by reconstitution of fractions into liposomes and measurement of sucrose uptake into the proteoliposomes. In addition, a mono-clonal antibody raised against tonoplast inhibited sucrose uptake. Western blots showed that the monoclonal antibody was relatively nonspecific but was suitable for monitoring the sucrose transport-related polypeptide during purification. The mono-clonal antibody bound a polypeptide of approximately 40 kDa, and this band was found in the fraction with sucrose uptake activity.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a697d521e6d5c6ab92722259acd9023 https://doi.org/10.1111/j.1399-3054.1992.tb01318.x Zobrazit plný text záznamu Plný text