title: [Serratia marcescens endonuclease. Properties of the enzyme].
abstract: Some physico-chemical properties of endonuclease (EC 3.1.4.9) from Serratia marcescens were studied and the amino acid composition of the enzyme was determined. The protein molecule was shown to contain one SH-group and one S-S-bond, which renders it different from the well studied nuclease (EC 3.1.4.7) from Staph. pyogenes. The conditions for reconstitution of the S-S-bond by dithioerythritol for quantitative estimation of cysteine residues of the endonuclease molecule were selected. The N-terminal amino acid was found to be threonine. The UV spectra for the enzyme are typical for proteins; A 0,1% 1cm,280nm is 1.46, epsilon 25 degrees 280nm,pH7,4 is 47292 M-1 cm-1. The sedimentation coefficient in phosphate buffer sW, 20 degrees is 3.4 S, pI is 6.5 and 7.5.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D004226:Dithioerythritol / Q000494:pharmacology; D004706:Endodeoxyribonucleases; D004720:Endonucleases / Q000302:isolation & purification* / Q000378:metabolism; D004722:Endoribonucleases; D008970:Molecular Weight; D012706:Serratia marcescens / Q000201:enzymology*; D013056:Spectrophotometry, Ultraviolet
chemical_list: D000596:Amino Acids; D004226:Dithioerythritol; D004706:Endodeoxyribonucleases; D004720:Endonucleases; D004722:Endoribonucleases; C021835:Serratia marcescens nuclease
vernacular_title: Endonukleaza Serratia marcescens. Kharakteristika fermenta.