Purification of a 57kDa nuclear matrix protein associated with thiol:protein-disulfide oxidoreductase and phospholipase C activities.
Proteins of the internal nuclear matrix from chicken liver were fractionated, by chromatographic procedures, in non denaturing conditions. At least two fractions were present with phosphatidylinositol-specific phospholipase C and three with thiol:protein-disulfide oxidoreductase activity. A 57kDa protein was isolated which copurified with both these activities. Partial amino acid sequences showed a high degree of homology with a cytosolic protein previously identified as a phospholipase C and with a microsomal protein identified as a thiol:protein-disulfide oxidoreductase. Our finding leaves the question still unanswered of the real function of this protein, which for the first time has been isolated from the nuclear matrix.
Altieri
F
F
Department of Biochemical Sciences A. Rossi Fanelli, University La Sapienza, Rome, Italy.
Maras
B
B
Eufemi
M
M
Ferraro
A
A
Turano
C
C
D000595:Amino Acid Sequence; D000818:Animals; D034961:Antigens, Nuclear; D002645:Chickens; D007150:Immunohistochemistry; D008099:Liver / Q000737:chemistry* / Q000201:enzymology; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D015530:Nuclear Matrix / Q000737:chemistry*; D009687:Nuclear Proteins / Q000302:isolation & purification*; D011490:Protein Disulfide Reductase (Glutathione) / Q000302:isolation & purification*; D017386:Sequence Homology, Amino Acid; D010738:Type C Phospholipases / Q000302:isolation & purification*
D034961:Antigens, Nuclear; D046911:Macromolecular Substances; D009687:Nuclear Proteins; D011490:Protein Disulfide Reductase (Glutathione); D010738:Type C Phospholipases