Isolation and purification of histones from avian erythrocytes

Sanders, Lee A.; McCarty, Kenneth S.

doi:10.1021/bi00773a004

Cited by 26 publications

(15 citation statements)

References 31 publications

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“…The fractionation of the six major histones present in avian erythrocytes by a combination of techniques including selective extraction, oxidation, gel filtration, and ion-exchange chromatography is a complicated and time-consuming procedure [16]. The further purification and separation of H5 into both its variants by conventional ion-exchange chromatography can take several days [10,17].…”

Section: Introductionmentioning

confidence: 99%

A new h.p.l.c. isolation procedure for chicken and goose erythrocyte histones

Helliger

Lindner

Hauptlorenz

et al. 1988

Biochemical Journal

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Total chicken erythrocyte histones were separated by reversed-phase h.p.l.c. using a multi-step acetonitrile gradient in a very short time (35 min). The proteins were eluted in the following order: H1, H5, H2B, H2A.2, H4, H2A.1 and H3.2. Applying a special gradient system adapted for the separation of very-lysine-rich histones, chicken erythrocyte H5 was resolved into two subfractions. Their electrophoretic mobilities were identical in both SDS and acetic acid/urea/Triton polyacrylamide-gel electrophoresis, but different in free-flow electrophoresis. Amino-acid-sequence analyses revealed that the two components only differ with respect to position 15, one having glutamine in that position and the other arginine. A separation of histones prepared from goose erythrocytes disclosed no H5 subfractionation. Furthermore, histones obtained from anaemic-chicken blood were analysed by the above-mentioned h.p.l.c. conditions. An alteration in the relation of H1 to H5 was detected, but no further differences in the number and quantity of the histones and histone variants were observed as compared with the corresponding proteins processed from normal-chicken blood.

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Section: Introductionmentioning

confidence: 99%

A new h.p.l.c. isolation procedure for chicken and goose erythrocyte histones

Helliger

Lindner

Hauptlorenz

et al. 1988

Biochemical Journal

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“…Although histones IIb1 and IIb2 of trout differ little in arginine content from those of chicken (13), goose (23), and duck (31), they are both eluted more readily fro111 Amberlite CG-58, even ahead of the unoxidized histone I H H and associated IV. As expected, the amino acid cornpositions of histones IBI and IV do not differ significantly from those of other lower vertebrates (29,31,36,38,39).…”

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The Histones of Rainbow Trout Erythrocytes Include an Erythrocyte-Specific Histone

Miki¹,

Neelin²

1975

Can. J. Biochem.

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The erythrocyte histones of rainbow trout were compared with those of goose by polyacrylamide gel electrophoresis. A band analogous to goose erythrocyte-specific histone V, but not identical in relative mobility or quantity, was found to be a component of trout erythrocyte histone. A similar component was also found in carp erythrocyte histone, but it was absent from trout liver histone. To reveal this band clearly, it was advantageous to displace the histone III monomer by oxidation. To verify the character of this protein, each of the main erythrocyte histones of trout were purified by chromatography on Amberlite CG-50, eluted with guanidinium chloride, and then further purified by exclusion chromatography on Bio-Gel P-60. Amino acid compositions of corresponding trout and goose histones, including that of the erythrocyte-specific histone, were sufficiently similar to establish their analogous identities. In general, the chromatographic and electrophoretic properties of histones I, IIb1, IIb2, and V from trout differed more from those of goose, than did their gross amino acid compositions. Comprehensive fractionation and characterization is necessary to extablish identities of corresponding histone fractions, An extensive quantitative variability was found among erythrocyte-specific histones of fish. This must be reconciled with hypothetical roles for this histone in erythropoiesis.

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“…This method is capable of separating previously unfractionable histones such as fish gonadal tissue, Arbacia punctulara sperm, T he widening scope of histone investigations has increased the demand for purified histone fractions for chemical and physical studies. Several lengthy procedures have been developed to produce both large amounts of a specific pure fraction of histone (Kinkade and Cole, 1966;Fambrough and Bonner, 1969;Iwai and Senshu, 1969;Mauritzen et al, 1966;Sanders and McCarty, 1972) and individual separation of all histone fractions from a given creature or tissue (Johns, 1964;Oliver et al, 1972). All methods are tedious and lengthy, requiring either multiple extractions with various aqueousorganic solvents or extensive column chromatography.…”

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confidence: 99%