Purification of a sensory-specific protein of 35 kDa (SSP-35).
Protein purification is a key technique for the identification of novel sensory nerve-specific proteins. A 35 kDa protein, the sensory neuronal specific protein, was isolated and purified from rabbit spinal ganglia and sensory fibers by homogenizing and deriving soluble extracts, followed by ion exchange chromatography using DEAE-Sephacel and gel filtration HPLC. Western blot analysis showed that the protein was present in spinal sensory ganglia but not in spinal motor neurons with anti-rat 35 kDa protein polyclonal antibody. The sensory-specific protein 35 kDa is termed SSP-35 in this paper. We found that the purified SSP-35 promoted axonal growth of the dorsal root ganglia of chick E8 embryos. Our data reveal that the protocol is an effective method for the purification of SSP-35. The protein may not only be a useful marker for sensory neurons, but also a possible tool to study the regeneration and function of sensory neurons.
Ping
X P
XP
National Key Research Laboratory of Natural and Biomimetic Drugs, Beijing Medical University, PR China. puxiaoping@263.net
Wang
J Z
JZ
D000818:Animals; D001369:Axons; D002455:Cell Division; D002642:Chick Embryo; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005727:Ganglia, Spinal / Q000378:metabolism*; D008297:Male; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000302:isolation & purification*; D009474:Neurons / Q000166:cytology / Q000378:metabolism; D011817:Rabbits
D009419:Nerve Tissue Proteins