[Isolation of nitrile hydratase from Rhodococcus rhodochrous M8 cells and determination of the N-terminal amino acid sequence of its subunits].
Nitrile hydratase was isolated and purified to homogeneity from cells of Rhodococcus rhodochrous M8. This enzyme catalyzes the hydrolysis of acrylic acid nitrile to acrylamide. Nitrile hydratase content in the cell was shown to be 17% of total soluble protein. The molecular weight of the native enzyme was 510 kDa. The enzyme consisted of two subunits with molecular weights of 23.5 kDa and 28.0 kDa. The N-terminal amino acid sequences of these subunits were estimated.
Sinolitskiĭ
M K
MK
Poltavskaia
S V
SV
Rogacheva
S M
SM
Sevriugina
I V
IV
Voronin
S P
SP
D000595:Amino Acid Sequence; D002849:Chromatography, Gas; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D006836:Hydro-Lyases / Q000737:chemistry / Q000302:isolation & purification*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012240:Rhodococcus / Q000201:enzymology*
D006836:Hydro-Lyases; C048831:nitrile hydratase