Comparison of histones from avian erythroid tissues by zone electrophoresis

Purkayastha, R. P.; Neelin, J. M.

doi:10.1016/0304-4165(66)90400-4

Cited by 54 publications

(14 citation statements)

References 17 publications

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“…Goose erythrocytes were obtained as described previously (19). IsoBation qf Cell Nuclei Cell lysis was accomplished by adjusting the cell suspension to 8.6% (w/v) saponin (British Drug Houses), then stirring for 30 min at 4 'C.…”

Section: Blood Collectionmentioning

confidence: 99%

“…Goose erythrocyte nuclei were obtained as described previously (19). Liver nuclei were isolated from 2 g fresh trout liver by homogenization for 45 s at medium speed on a Virtis '23' homogenizer (Gardiner, N.Y.), in 18-20 volumes of Cortland's solution made hypertonic with 0.32 M sucrose.…”

Section: Blood Collectionmentioning

confidence: 99%

“…The nuclear residue was separated by centrifugation at 12 000 X g (average) and the combined supernatants were clarified by centrifugation at 17 3 0 X g (average) for 20 min. Whole goose erythrocyte histone was obtained as described previously (19).…”

Section: Hissane Extr-action and C/wrnical Leaodijcarionmentioning

confidence: 99%

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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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Section: Blood Collectionmentioning

confidence: 99%

Section: Blood Collectionmentioning

confidence: 99%

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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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“…A current of 16-20 mA was applied for 6.5 h at room temperature. On staining with Amido black (14) five protein bands, two major and three minor, were detected. All were basic proteins.…”

Section: Exaniitiatio~z Of Proteasementioning

confidence: 99%

Isolation and preliminary characterization of an extracellular protease of Cytophaga sp.

Christison¹,

Martin²

1971

Can. J. Microbiol.

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CHRISTISON, J., and S. M. MARTIN. 1971. Isolation and preli~ninary characterization of an extracellular protease of Cytoplraga sp. Can. 3. Microbial. 17: 1207-1216. The extracellular protease(s) of Cytopl~aga sp. is present naturally as a complex with acidic polysaccharides of the slime layer. The protein was separated from the slime by selective precipitation of the polysaccharide with a cationic detergent and the enzyme was purified about 100-fold by precipitation with alcohol and by chroinatography on DEAE-cellulose. Inhibitor studies indicated that this alkaline protease was not of the trypsin/chymotrypsin type. Ca2+ had a strong stabilizing effect on the enzyme. The coinplex of basic protein (enzyme) and acidic slime polysaccharides has led to the conclusion that the enzyme is perhaps not truly extracellular but rather is surface bound. The slime layer would appear to have a role in attaching the bacterial cells to insoluble substrates as well as ensuring that degradative enzymes are kept in close contact with the substrate.La proteinase exocellulaire de Cytoplraga sp. est naturellement complexte avec les polysaccharides acidifiants formant la couche de mucus. La prottine fut skparee du mucus par precipitation selective des polysaccharides avec un dttergent cationique et l'enzyme fut purifiC environ 100 fois par precipitation a I'alcool et par chronlatographie sur DEAE-cellulose. Des etudes d'inhibition ont indiqut que cette proteinase alcaline n'est pas du type trypsine/chymotrypsine. Le Ca2+ a un grand pouvoir stabilisant sur l'enzyme. Le complexe de prottines basiques (enzyme) et le mucus acidifiant de polysaccharides portent a conclure que l'enzyme n'est peut-&re pas rtellement exocellulaire, mais serait plutbt attache a la surface cellulaire. La couche de mucus aurait alors comme rble d'attacher les cellules bacttriennes aux substrats insolubles aussi bien qne de maintenir les enzymes de degradation en etroit contact avec le substrat.

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“…Or le sang du poussin contient plus de stades jeunes [S] de la lignee Brythroide que l'adulte, oh I'on ne trouve presqu'exlusivement que des Brythrocytes mtirs. De mbme, la moelle osseuse ob l'on a toutes les Btapes de maturation des cellules sanguines, contiendrait peu d'histone specifique [6] et apres un traitement anemiant 1 la phenylhydrazine, elle n'en contiendrait plus [7] . I1 se pourrait que la presence d'histone specifique soit reliee directement au degre de maturation des cellules nuclees de la lignee rouge.…”

Section: Chromatographyunclassified

Variation quantitative de la fraction d'histone specifique aux erythrocytes, au cours du developpement du poulet

Mazen

Champagne

1969

FEBS Letters

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Recu le 11 janvier 1969Chromatography on carboxymethylcellulose of the trichloracetic extract "Fr" of chicken erythrocytes nuclei, yields two histone fractions: F t-cF t the very lysine-rich histone and F r-cFs, the fraction specific to erythrocytes.Aminoacid analysis and disc electrophoresis on extracts "F 1" demonstrate that specific histone fraction F r-cFs occurs in smaller percentage in the early stages of chicken development; it increases from 6% (by weight of the total DNA) in 3 days old chicken to 16% in 21 days old chicken. But the percentage of F r-cFr fraction (8% by weight of total DNA) remains constant in the same conditions.

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Comparison of histones from avian erythroid tissues by zone electrophoresis

Cited by 54 publications

References 17 publications

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

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

Isolation and preliminary characterization of an extracellular protease of Cytophaga sp.

Variation quantitative de la fraction d'histone specifique aux erythrocytes, au cours du developpement du poulet

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