PubMed · 3704178
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J Sugatani, T Okumura, K Saito. 1986. [Phospholipase B].. https://pubmed.ncbi.nlm.nih.gov/3704178/
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A novel molybdenum-free nitrate reductase was isolated from the obligate chemolithoautotrophic and facultative anaerobic, (halo)alkaliphilic sulphur-oxidizing bacterium Thioalkalivibrio nitratireducens strain ALEN 2. The enzyme was found to contain vanadium and haem c as cofactors. Its native molecular mass was determined as 195 kDa, and the enzyme consists of four identical subunits with apparent molecular masses of 57 kDa. Apart from nitrate, the enzyme can utilize nitrite, chlorate, bromate, selenate and sulphite as electron acceptors. Moreover, it also has a haloperoxidase activity.
We examine distribution of flagellins along multicomponent flagellar filaments (FF) and protofilaments (PF) of the haloalkaliphilic archaeon Natrialba magadii using immunogold electron microscopy. A high specific polyclonal antibody raised to one of the flagellin types bound homogeneously to the undissociated FF along the full length. At the same time both uniformly labelled and completely unlabelled PF, outwardly indistinguishable one from another, were observed.
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