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1.
J Mol Biol ; 244(1): 114-6, 1994 Nov 18.
Article in English | MEDLINE | ID: mdl-7966315

ABSTRACT

Poly (ADP-ribose) polymerase (PARP) participates in the immediate response in mammalian cells exposed to DNA-damaging agents. Recombinant baculovirus harboring the cDNA of the chicken PARP catalytic domain (40 kDa) have been used to infect Spodoptera frugiperda (Sf9) insect cells. The recombinant polypeptide (30 mg per 1 x 10(9) cells) was purified to homogeneity by 3-aminobenzamide affinity chromatography. The enzymatic properties of the recombinant domain were similar to those of the native fragment. Crystals of the purified recombinant catalytic domain were grown by vapor diffusion. The crystals belong to space group P2(1)2(1)2(1) with unit cell dimensions of a = 59.2 A, b = 65.0 A, c = 96.9 A. They are suitable for X-ray analysis and diffract to 2.0 A.


Subject(s)
Poly(ADP-ribose) Polymerases/chemistry , Animals , Baculoviridae/genetics , Base Sequence , Binding Sites , Chickens , Chromatography, Affinity , Crystallography, X-Ray , Molecular Sequence Data , Peptide Fragments/chemistry , Poly(ADP-ribose) Polymerases/genetics , Poly(ADP-ribose) Polymerases/isolation & purification , Recombinant Proteins/chemistry , Recombinant Proteins/isolation & purification , Spodoptera/cytology
2.
Nucleic Acids Res ; 1(8): 1043-57, 1974 Aug.
Article in English | MEDLINE | ID: mdl-10793734

ABSTRACT

In native nucleoprotein, the premelting structural changes of DNA are not observed by circular dichroism measurements. In order to determine which protein fraction of chromatin is responsible for the absence of premelting we have examined a series of nucleoproteins depleted of different protein fractions by treatment with sodium chloride or sodium deoxycholate.The premelting reappears as soon as non-histone proteins are removed or in residual complexes from which the two slightly lysine-rich histone fractions (F2a2+F2b) have been removed. On the other hand, it is shown that histone F1 alone is not able to suppress the premelting phenomenon. It is thus concluded that the absence of premelting is a property of native nucleoprotein where interactions between the different proteins complexed with DNA can occur and especially between the non-histone proteins and the two slightly lysine-rich histone fractions.


Subject(s)
Nucleoproteins/chemistry , Animals , Cattle , Chromatin/chemistry , Chromatin/isolation & purification , Chromosomal Proteins, Non-Histone/chemistry , Chromosomal Proteins, Non-Histone/isolation & purification , Circular Dichroism , Histones/isolation & purification , In Vitro Techniques , Lysine/analysis , Nucleoproteins/isolation & purification , Protein Conformation , Protein Denaturation , Spectrophotometry, Ultraviolet
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