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Purification of colored photosynthetic proteins for understanding protein isolation principles
Author(s) -
Bes M. Teresa,
Sancho Javier,
Peleato M. Luisa,
Medina Milagros,
GómezMoreno Carlos,
Fillat María F.
Publication year - 2003
Publication title -
biochemistry and molecular biology education
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.34
H-Index - 39
eISSN - 1539-3429
pISSN - 1470-8175
DOI - 10.1002/bmb.2003.494031020202
Subject(s) - ferredoxin , isolation (microbiology) , biochemistry , spinach , computational biology , protein purification , reductase , biology , biochemical engineering , chromatography , chemistry , enzyme , bioinformatics , engineering
The purification of a protein is the essential initial step in the study of its physical and biological properties and is one of the most common procedures in biochemistry. This article describes a method for teaching purification skills through the partial isolation of ferredoxin‐NADP + reductase and ferredoxin from a single cell batch. The method has been used for several years in an introductory biochemistry course using spinach leaves as cellular source. The protocol gives a complete picture of the preparation of a crude extract and the subsequent isolation of both electron transport proteins on a laboratory scale. It introduces students to the use of different techniques for the purification and detection of proteins and allows them to develop a number of valuable experimental and analytical skills without necessarily resorting to complicated or expensive equipment.