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Two Acidic Proteins Associated with Brain Development in Chick Embryo
Author(s) -
Shirao Tomoaki,
Obata Kunihiko
Publication year - 1985
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1985.tb08745.x
Subject(s) - isoelectric focusing , biology , gel electrophoresis , embryogenesis , staining , isoelectric point , biochemistry , peptide , embryo , protease , microbiology and biotechnology , embryonic stem cell , polyacrylamide gel electrophoresis , two dimensional gel electrophoresis , silver stain , electrophoresis , gene , proteomics , genetics , enzyme
The developmental changes in protein composition of the chick optic tectum were analyzed by twodimensional gel electrophoresis. Staining with Coomassie Brilliant Blue R revealed 54 major proteins, eight of which remarkably changed their abundance during development: Four of these proteins (S8, S14, S30, and S54) increased and two of them (S7 and S37) decreased in the course of the brain development. The other two proteins (S5 and S6) appeared at specific embryonic stages and were not detected in the adult. The abundance of S5 protein was highest at day 7, and that of S6 protein at days 9–18. The two proteins were present in other regions of the embryonic brain but were not detected in the embryonic liver. The proteins were purified from the soluble fraction of embryonic chick brains by pH 5.5 precipitation, DEAE‐Sepharose column chromatography, ammonium sulfate precipitation, and sodium dodecyl sulfatepolyacrylamide gel electrophoresis. The molecular weights of S5 and S6 proteins were 95,000 and 100,000, respectively, and their isoelectric points were about 4.5. They were compared by peptide mapping using V8 protease and found to share 11 common peptides out of 17 distinct ones. This indicates a strong degree of structural homology between these two proteins.