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Identity Between Cytoplasmic and Membrane‐Bound S‐100 Proteins Purified from Bovine and Rat Brain
Author(s) -
Donato Rosario,
Prestagiovanni Bruno,
Zelano Giovanni
Publication year - 1986
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.1471-4159.1986.tb01743.x
Subject(s) - cytoplasm , membrane , membrane protein , biology , biochemistry , chemistry
Cytoplasmic and membrane‐bound S‐100 proteins were purified to homogeneity from bovine and rat brain. Cytoplasmic and membrane‐bound S‐100 from single species are identical by immunological, electrophoretic, spectrophotometric, and functional criteria. Cytoplasmic and membrane‐bound S‐100 from bovine brain consists of nearly equal amounts of S‐100a and S‐100b, whereas cytoplasmic and membrane‐bound S‐100 from rat brain consists mostly of S‐100b. The functional role of membrane‐bound S‐100 remains to be elucidated.