Corynebacterium glutamicum R adhA gene encodes a homodimeric, NAD-dependent, 345 amino acid residue alcohol dehydrogenase with two zinc ions per subunit. Chromosomal inactivation of the adhA gene rendered the strain incapable of growth on either ethanol or n-propanol as the sole carbon source. RNA hybridization analysis revealed that adhA transcription was not only induced by these two substrates, but it was also subject to glucose catabolite repression. Accordingly, both induction of AdhA activity and ethanol utilization were detected only after depletion of glucose. Deletion of either or both of potential cyclic adenosine monophosphate (cAMP) receptor binding site and an inverted repeat of sequence 5'-GCAATTGATG-N (8)-CACAATTGC-3' in the promoter region of adhA strongly suggested that IR, which does not share significant similarity with other regulatory DNA elements of C. glutamicum, represents a transcriptional repressor binding site. Purified recombinant AdhA displayed the highest substrate specificities towards ethanol and n-propanol and their corresponding aldehydes.
Visfatin was originally described as an adipokine with insulin
mimetic effects. Recently, it was found that visfatin is identical
with the Nampt (nicotinamide phosphoribosyltransferase) gene
that codes for an intra- and extracellular NAD biosynthetic
enzyme and is predominantly expressed outside the adipose
tissue. In the current study, we found strong protein and mRNA
expression of visfatin in rat heart, liver, kidney, and muscle, while
the expression of visfatin in visceral fat was significantly lower
and undetectable in subcutaneous fat. The insulin-mimetic
effects of visfatin (extracellular form of Nampt or eNampt) are
controversial and even less is known about autocrine effects of
visfatin (intracellular form of Nampt or iNampt). Since liver plays
a major role in glucose metabolism, we studied visfatin effects on
insulin-stimulated cellular glucose uptake in Fao rat hepatocytes
using RNA interference (RNAi). RNAi-mediated downregulation of
visfatin expression in Fao cells was associated with significantly
reduced NAD biosynthesis (0.3±0.01 vs. 0.5±0.01 mmol/h/g,
P<0.05) and with significantly decreased incremental glucose
uptake after stimulation with insulin when compared to controls
with normal expression of visfatin (0.6±0.2 vs. 2.2±0.5
nnmol/g/2 h, P=0.02). These results provide evidence that
visfatin exhibits important autocrine effects on sensitivity of liver
cells to insulin action possibly through its effects on NAD
biosynthesis.
The content of eggs and egg white, respectively, in various foods (pastes, mayonnaises, dressings, confections containing egg white, various ready-tocook mixtures, ice creams, omelettes, custards, pie Jillings etc) was assessed by radial immunodiffusion and preferably by rocket immunoelectrophoresis. The problem of partial ovalbumin denaturation during processing of dried eggs or egg white was overcome by using these products for the calibration of the method used. The method may also be applied to assess the degree of egg white contamination in mayonnaises in order to control the yolk and egg tyhite separation during processing.
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