
X-ray diffraction based model showing Spinach RuBisCO in complex with 2-carboxyarabinitol 2 bisphosphate and calcium.
Similar to the situation of plasma or serum proteomics, plant proteomics study also faces the challenges of specifically removing the HAP from plant protein extract in order to analyze or detect the LAP.
RuBisCO (Ribulose-1,5-bisphosphate carboxylase/oxygenase) is the most abundant protein in plants, and it may be the most abundant protein on Earth. RuBisCO is an enzyme that is used in the Calvin cycle to catalyze the first major step of carbon fixation, a process by which the atoms of atmospheric carbon dioxide are made available to organisms in the form of energy-rich molecules such as sucrose. RuBisCO, while being the key enzyme in photosynthetic carbon assimilation in green leaves, is the main obstacle in plant proteomics. It constitutes about 40% of the total protein mass in green leaves, thus interfering with proteomics studies such as LC-MS/MS and 2D-gel electrophoresis. To meet the needs for specifically and effectively separating RuBisCO from other plant proteins, the novel immunoaffinity matrix based on the IgY antibodies cross-linked to microbeads, which specifically removes RuBisCO protein from plant extract was developed.
Seppro® RuBisCO Column Features:
X-ray diffraction based model showing Spinach RuBisCO in complex with 2-carboxyarabinitol 2 bisphosphate and calcium.
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