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Biotechnology and Applied Biochemistry (1998) 28, (215–218) (Printed in Great Britain)

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An improved, inexpensive method for the large-scale purification of human nerve growth factor

Suqin Li¹, Faqing Li, Weiguo Tan, Nan Yang, Huiying Jin and Huabiao Chen

Huadong Research Institute for Medical Biotechnics, 293 East Zhongshan Road, Nanjing 210002, Peoples' Republic of China

¹To whom correspondence should be addressed.

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.

Received 23 February 1998/11 June 1998; accepted 16 June 1998

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