[Serratia marcescens nucleases. II. Primary structure analysis by peptide mapping combined with plasma-desorption mass spectrometry].
The primary structures of nucleases Sm1, Sm2, and Sm3 produced by Serratia marcescens were completely characterized using plasma desorption mass spectrometry (PDMS) of proteolytic peptides isolated by reverse-phase HPLC. The isoforms were separated by anion-exchange chromatography on DEAE cellulose and subjected to hydrolysis by the lysine-specific endoproteinase Lys-C. Comparative analysis of the peptides identified by PDMS showed that all three nucleases are N-terminal variants of the same protein: Sm2 represents a "mature" protein form, whereas Sm1 and Sm3 lack three and one N-terminal amino acid residues, respectively.
Pedersen
J
J
Department of Biotechnology, Danish Technical University, Lingbi.
Filimonova
M N
MN
Roepstorff
P
P
Bidermann
K
K
D000595:Amino Acid Sequence; D002848:Chromatography, DEAE-Cellulose; D002851:Chromatography, High Pressure Liquid; D004706:Endodeoxyribonucleases / Q000737:chemistry*; D004722:Endoribonucleases / Q000737:chemistry*; D006868:Hydrolysis; D007525:Isoelectric Focusing; D013058:Mass Spectrometry / Q000379:methods*; D008666:Metalloendopeptidases / Q000737:chemistry; D008969:Molecular Sequence Data; D010449:Peptide Mapping
D004706:Endodeoxyribonucleases; D004722:Endoribonucleases; C021835:Serratia marcescens nuclease; D008666:Metalloendopeptidases; C039830:peptidyl-Lys metalloendopeptidase
Nukleazy Serratia marcescens. II. Analiz pervichnykh struktur putem peptidnogo kartirovaniia v kombinatsii s plazmenno-desorptsionnoĭ mass-spektrometrieĭ.