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An improved, inexpensive method for the large‐scale purification of human nerve growth factor
Author(s) -
Li Suqin,
Li Faqing,
Tan Weiguo,
Yang Nan,
Jin Huiying,
Chen Huabiao
Publication year - 1998
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1111/j.1470-8744.1998.tb00532.x
Subject(s) - monoclonal antibody , nerve growth factor , recombinant dna , chromatography , chemistry , western blot , isoelectric point , isoelectric focusing , affinity chromatography , antibody , biochemistry , biology , immunology , receptor , enzyme , gene
Human nerve growth factor (hNGF) was purified to near homogeneity on a large scale from human term placenta with an improved and inexpensive method. The purification procedure included tissue homogenization, ultrafiltration and single CM‐cellulose column chromatography. The purified hNGF was a 14·4‐kDa protein with an isoelectric point of approximately 9·3. The specific activity of the purified hNGF was approximately 38000 units/mg, and the activity was completely inhibited by the monoclonal antibody against recombinant hNGF (rhNGF). Western‐blot analysis showed that the purified hNGF could interact with the monoclonal antibody against rhNGF.