TY - JOUR
T1 - A rapid purification of synapsin I
T2 - A neuron specific spectrin binding protein
AU - Krebs, K. E.
AU - Zagon, I. S.
AU - Goodman, S. R.
N1 - Funding Information:
This project was supported in part by National institutes of Health Grants NS-19357a nd HL-26059t o S. R. Goodmana nd NS-21246t o I. S. Zagon and S. R. Goodman. S. R. Goodman is an Established investigatoro f the American Heart Association. We thank Dr. Paul Greengardf or his gift of bovine synapsinf , and Ms. Anne Karinch for the gift of F-actin. We thankM s. Bonnie McAvoy for her excellentt echnicala ssistance.a nd Mr. David Sitler for the photography.
PY - 1986/8
Y1 - 1986/8
N2 - We have developed a one Chromatographic step isolation protocol for the neuron specific protein synapsin I. This procedure results in a yield of 80 μg/g brain, which is ten fold better than the highest yield yet reported for this protein. The authenticity of the synapsin I isolated by this procedure is demonstrated by comigration with authentic synapsin I on SDS-polyacrylamide gels, crossreactivity with antibody specific against synapsin I, and nearly identical two dimensional chrymotryptic iodopeptide maps of authentic synapsin I and the protein purified by this protocol. Synapsin 1 isolated by this procedure retains its functional properties, demonstrated by the ability of synapsin I to stimulate the formation of a brain spectrin(240/235)/synapsin I/F-actin ternary complex as determined by a low shear falling ball viscometry assay. This novel protocol therefore has the advantage of being a rapid, high yield procedure that retains the functional properties of synapsin I.
AB - We have developed a one Chromatographic step isolation protocol for the neuron specific protein synapsin I. This procedure results in a yield of 80 μg/g brain, which is ten fold better than the highest yield yet reported for this protein. The authenticity of the synapsin I isolated by this procedure is demonstrated by comigration with authentic synapsin I on SDS-polyacrylamide gels, crossreactivity with antibody specific against synapsin I, and nearly identical two dimensional chrymotryptic iodopeptide maps of authentic synapsin I and the protein purified by this protocol. Synapsin 1 isolated by this procedure retains its functional properties, demonstrated by the ability of synapsin I to stimulate the formation of a brain spectrin(240/235)/synapsin I/F-actin ternary complex as determined by a low shear falling ball viscometry assay. This novel protocol therefore has the advantage of being a rapid, high yield procedure that retains the functional properties of synapsin I.
UR - https://www.scopus.com/pages/publications/0022449913
UR - https://www.scopus.com/pages/publications/0022449913#tab=citedBy
U2 - 10.1016/0361-9230(86)90120-6
DO - 10.1016/0361-9230(86)90120-6
M3 - Article
C2 - 3094836
AN - SCOPUS:0022449913
SN - 0361-9230
VL - 17
SP - 237
EP - 241
JO - Brain Research Bulletin
JF - Brain Research Bulletin
IS - 2
ER -