The Fractionation of Arginine-rich Histones from Fetal Calf Thymus by Exclusion Chromatography

Mauritzen, C. M.; Starbuck, Wesley C.; Saroja, Iengar S.; Taylor, Charles W.; Busch, Harris

doi:10.1016/s0021-9258(18)96040-0

Cited by 51 publications

(6 citation statements)

References 16 publications

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“…Histones ARE, GRK, LAK, and KAS from calf thymus were purified by published methods (Ruiz-Carrillo and Allfrey, 1973;Mauritzen et al, 1967;Sugano et al, 1972;Senshu and Iwai, 1970). They were electrophoretically pure (Panyim and Chalkley, 1969), and the amino acid analyses agreed with the sequences (DeLange et al, 1972, Ogawa et al, 1969Yeoman et al, 1972;Iwai et al, 1970).…”

Section: Methodsmentioning

confidence: 99%

Histone cross-complexing pattern

D'Anna¹,

Isenberg²

1974

Biochemistry

241

133

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al residues per tetramer go into an -helical conformation. Complexing inhibits the slow aggregation of ARE and GRK. Histones ARE and LAK also interact in a 1:1 molar ratio, but there is no increased a helicity upon complexing, and slow aggregation and /3-sheet formation occur. ARE and KAS also interact, but, upon complexing, there is no change in the tyrosine rigidity or in the circular dichroism. A pattern of the interactions between LAK, KAS, ARE, and GRK is presented. more weakly (D'Anna and Isenberg, 1974a). The complexes require salt for stability and, in fact, they were formed by adding salt to histone mixtures in water. One or both of the partner histones in the strong complexes, KAS-GRK and LAK-KAS, show marked conformational changes upon complexing, and the complex shows considerably more -helical content than the uncomplexed molecules.Skandrani et al. (1972) and Kelley (1973) have also reported a 1:1 complex of histones LAK and KAS, which was isolated by chromatographic fractionation of mixed his-4992 BIOCHEMISTRY, VOL.

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Section: Methodsmentioning

confidence: 99%

Histone cross-complexing pattern

D'Anna¹,

Isenberg²

1974

Biochemistry

241

133

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“…This purified histone preparation was fractionated by electrophoresis on polyacrylamide gels (14) . For each gel tube of 4 mm (ID) X 90 mm (L), 3 ma current was applied and electrophoresis was carried out in the cold at 4 °-6°C for 2 hr.…”

Section: Extraction and Acrylamide Gel Electrophoresis Of Histonesmentioning

confidence: 99%

Isolation of Nuclei From Yeast

Bhargava

Halvorson

1971

The Journal of Cell Biology

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A method for isolation of nuclei from Saccharomyces cervisiae in high yield is described. The DNA/protein ratio of the isolated nuclei is 10 times higher than that of whole cells. Examination of these nuclei in phase and electron microscopes has shown them to be round bodies having a double membrane, microtubules, and a dark crescent at one end. The optimum conditions for extraction and resolution of histones of these nuclei on acrylamide gels have been investigated. The nuclei have an active RNA polymerase (E.C. 2.7.7.6) and are able to synthesize RNA in vitro. They are also readily stainable with Giemsa's, Feulgen's, and acridine orange methods.

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“…The values are expressed as mol of each amino acid/lOOmol of amino acids recovered. The amounts of threonine, serine and tyrosine have been corrected for destruction during hydrolysis (Mauritzen et at. 1967).…”

Section: Resultsmentioning

confidence: 99%

“…However, it is still unclear as to whether all histones are aligned to neutralize the phosphate groups of DNA, or whether some histones are specifically linked to specific base sequences, as suggested by the close relationship described between G+C-rich components of DNA and histones (Crampton, Lipschitz & Chargaff, 1954; Skalka, Rasmussen & Luck, 1964). Elucidation of such problems is now possible since precise methods for the isolation and characterization of individual histone species have been developed (Johns, 1967;Mauritzen, Starbuck, Taylor, Saroja & Busch, 1967;). Extensive investigations on the primary structure of histones are being made, and some preliminary results have been reported (Desai, Ogawa, Mauritzen, Taylor & Starbuck, 1969; Sautiere, Starbuck, Roth & Busch, 1968; DeLange, Fambrough, Smith & Bonner, 1968).…”

mentioning

confidence: 99%

“…with Phenol Red as a marker. The chromatographic sheet was air-dried and subjected to high-voltage electrophoresis with arginine as a marker, with pyridine-acetate buffer, pH 3.6 (Katz, Dreyer & Anfinsen, 1959;Mauritzen et al 1967). The chromato-electrophoretic sheets were dipped in ninhydrincadmium reagent (Liu, Stein, Moore & Elliott, 1965) to locate peptides (spots) and the arginine-containing peptides were identified with Sakaguchi reagent (Canfield & Anfinsen, 1963).…”

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confidence: 99%

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Homologies in amino acid composition and structure of histone F2al isolated from human leukaemic cells

Desai

Foley

1970

Biochemical Journal

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Histones F2al extracted from normal and neoplastic cells possess similar amino acid compositions. Tryptic and chymotryptic peptides of the F2al histones have identical chromato-electrophoretic R(F) values. It is concluded that histones F2al from various sources have similar overall structures. The observed differences in the ratios of in-N-monomethyl- and di-in-N-methyl-lysine in the histones from normal and neoplastic cells may be of significance with respect to gene regulation.

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The Fractionation of Arginine-rich Histones from Fetal Calf Thymus by Exclusion Chromatography

Cited by 51 publications

References 16 publications

Histone cross-complexing pattern

Histone cross-complexing pattern

Isolation of Nuclei From Yeast

Homologies in amino acid composition and structure of histone F2al isolated from human leukaemic cells

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