N-terminal heterogeneity of methylamine dehydrogenase from Thiobacillus versutus.
The N-terminal processing of MADH from the bacterium T. versutus and the N-terminal heterogeneity of the isolated alpha subunit of the alpha 2 beta 2 protein complex was demonstrated by a combination of Edman sequence analysis of an electroblotted band, in situ digested with pyroglutamate aminopeptidase, and accurate mass determination of the homogeneous subunit by the technique of electrospray ionisation mass spectrometry. From this study, it appears that the corresponding gene of the alpha subunit contains 395 amino acids and that it is preceded by a leader sequence of 31 residues.
Van Beeumen
J
J
Department of Biochemistry, Physiology and Microbiology, University of Gent, Belgium.
Van Driessche
G
G
Huitema
F
F
Duine
J A
JA
Canters
G W
GW
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry* / Q000235:genetics; D011751:Pyroglutamyl-Peptidase I; D013855:Thiobacillus / Q000201:enzymology*
C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D011751:Pyroglutamyl-Peptidase I