IgY RuBisCO Columns

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:

  • High-efficiency RuBisCO removal
  • High column capacity
  • Successfully applied for processing a variety of plant samples

X-ray diffraction based model showing  Spinach RuBisCO in complex with  2-carboxyarabinitol 2 bisphosphate  and calcium

X-ray diffraction based model showing  Spinach RuBisCO in complex with  2-carboxyarabinitol 2 bisphosphate  and calcium.

 

Product Name Use Capacity of RuBisCO protein Product No.
Anti-RuBisCO Spin Columns
Includes 2 spin columns
100 times 0.2 mg SEP070
Anti-RuBisCO HPLC LC-2 column
Includes 1 HPLC column
100 times 1 mg SEP080

 

 Reference

  • Cellar NA, Kuppannan K, Langhorst ML, Ni W, Xu P, Young SA. (2007). Cross species applicability of abundant protein depletion columns for ribulose-1,5-bisphosphate carboxylase/oxygenase. J Chromatogr B Analyt Technol Biomed Life Sci. Epub.

 

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