| Autor: |
McDonald HC, Takeguchi MM, Detar CC, Simon PA, Livsey KA, Odstrchel G, Kaplan NO, Weetall HH |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of general microbiology [J Gen Microbiol] 1980 Aug; Vol. 119 (2), pp. 451-8. |
| DOI: |
10.1099/00221287-119-2-451 |
| Abstrakt: |
An enzyme which oxidizes 1,2-propanediol in the presence of NAD+ has been purified from lysates of Neisseria gonorrhoeae. The enzyme was activated by monovalent cations, had a pH optimum between 9 and 10, and showed a substrate specificity unlike any known alcohol or glycerol dehydrogenase. The enzyme had an apparent Km of 17 mM for 1,2-propanediol and 0 . 37 mM for NAD+. When chromatographed on a Sephadex G-150 column, the enzyme eluted as a single peak in the molecular weight region of a bovine serum albumin marker. An antibody to the purified enzyme was prepared in goats. When antiserum was reacted with the enzyme in immunodiffusion experiments, a single precipitin band was detected. When the enzyme was mixed with an excess of antibody and then reacted with substrate, enzyme activity was completely inhibited. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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