[Properties of protein released from mouse spleen nuclei under conditions of limited hydrolysis with DNase I and micrococcal nuclease].
Proteins released by mouse spleen nuclei under conditions of limited hydrolysis with DNase I and micrococcal nuclease were compared. Analysis of these proteins by polyacrylamide gel electrophoresis in the presence of SDS revealed the essential similarity in the qualitative composition of released proteins. Characteristics of the most prominent component were studied in both cases and it was shown that this component is identical. It has a molecular weight of 25 500 according to electrophoresis data and 2300 as determined by equilibrium sedimentation. Amino acids composition and N-terminal amino acid were studied. It was shown that its N-amino acid is arginine.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002467:Cell Nucleus / Q000032:analysis*; D003850:Deoxyribonuclease I; D003851:Deoxyribonucleases; D004591:Electrophoresis, Polyacrylamide Gel; D004720:Endonucleases; D006868:Hydrolysis; D051379:Mice; D008836:Micrococcal Nuclease; D008970:Molecular Weight; D009698:Nucleoproteins / Q000302:isolation & purification*; D013154:Spleen / Q000032:analysis*
D000596:Amino Acids; D009698:Nucleoproteins; D003851:Deoxyribonucleases; D004720:Endonucleases; D003850:Deoxyribonuclease I; D008836:Micrococcal Nuclease
Kharakteristika belka, vysvobozhdaemogo iz khromatina iader selezenki myshi v usloviiakh ogranichnnogo gidroliza DNKazoĭ I i mikrokokkovoi nukleazoĭ.