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Studies on Nuclei of Paramecium aurelia. II. Amino Acid Composition and Electrophoretic Properties of the Chromosomal Basic Proteins *
Author(s) -
ISAACKS R. E.,
SANTOS B. G.
Publication year - 1973
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1973.tb00931.x
Subject(s) - paramecium aurelia , paramecium , electrophoresis , histone , biochemistry , lysine , biology , sephadex , amino acid , polyacrylamide gel electrophoresis , chemistry , chromatography , microbiology and biotechnology , dna , enzyme
SYNOPSIS. The basic proteins of Paramecium aurelia nucleus were extracted from isolated nuclei and deoxyribonucleoprotein (DNP) of such nuclei. About 35–40% of the nuclear protein, predominantly a lysine‐rich histone, is acid soluble. Five major components of the histone can be distinguished by polyacrylamide gel electrophoresis. Some components of Paramecium histone are similar to those of mammalian histones in their electrophoretic mobility, but they differ from the latter in the electrophoretic velocity and relative levels. The basic to acidic amino acid ratio of the histone from the ciliate is ∼1.1–1.5, and its amino acid composition resembles closely that of yeast histone. Through the use of Sephadex G‐200 gel filtration for purification of the histones extracted directly from isolated nuclei 2 basic proteins were resolved—component I, with an elution volume of 1.4, constitutes ∼20% and component II, with an elution volume of 1.9, ∼80%.