ISSN:
1471-4159
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Medicine
Notes:
Abstract— The S-100 protein fraction of pig and sheep brain was purified in 40 per cent yield by a modification of the procedure of Moore (1965), which avoided selective loss of S-100 components. The S-100 fraction of both pig and sheep is a mixture of proteins as indicated by acrylamide gel electrophoresis and N-terminal amino acid analysis. Differences in amino acid composition, electrophoretic heterogenity and N-terminal analysis were found.One fraction (fraction A) was isolated by DEAE-Sephadex chromatography from pig brain S-100 protein fraction. It was considered to be a single protein since it migrated as a single band on acrylamide gel electrophoresis and showed a single symmetrical peak during ultracentrifugal analysis. Only one N-terminal amino acid was detected in fraction A. The amino acid composition of this fraction showed minor but significant differences from that of the complete S-100 protein fraction from pig brain. The S-100 protein fraction of both species, as well as fraction A, had similar s20, w values and similar molecular weights (about 20,000) as indicated by gel filtration. These results, together with the immunological data obtained by other authors, suggest that the proteins of the S-100 fraction are closely related; the heterogeneity of the S-100 protein fraction may be of the same type as the lactate dehydrogenase isoenzymes.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1471-4159.1971.tb11970.x
