An improved, inexpensive method for the large-scale purification of human nerve growth factor.
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.
Li
S
S
Huadong Research Institute for Medical Biotechnics, 293 East Zhongshan Road, Nanjing 210002, Peoples' Republic of China.
Li
F
F
Tan
W
W
Yang
N
N
Jin
H
H
Chen
H
H
D002681:China; D002852:Chromatography, Ion Exchange; D003363:Cost Control; D006801:Humans; D007118:Immunoassay; D007525:Isoelectric Focusing; D009414:Nerve Growth Factors / Q000302:isolation & purification*; D014462:Ultrafiltration
D009414:Nerve Growth Factors