Author:
Li Suqin,Li Faqing,Tan Weiguo,Yang Nan,Jin Huiying,Chen Huabiao
Abstract
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.
Subject
Process Chemistry and Technology,Drug Discovery,Applied Microbiology and Biotechnology,Biomedical Engineering,Molecular Medicine,General Medicine,Bioengineering,Biotechnology