Potentiometric Glycerol Biosensor Based On Immobilization Of Glycerol-Dehydrogenase On Au Using A Molecular Wiring System

The endogenous rate of glycerol production in rabbits was measured by several techniques: constant infusion of 1,3-14C-glycerol or 2-3H-glycerol or unlabeled glycerol; single injection of 1,3-14C-glycerol or 2-3H-glycerol or unlabeled glycerol. The rate was 5.5–11.6 μmoles/kg per minute (9 rabbits). The mean fractional turnover rate was 0.0585 ± 0.0052. During infusion of noradrenaline together with 3H-glycerol, the fractional turnover rate was no different from that in the absence of noradrenaline. The maximum utilization rate of glycerol was 28.1 ± 1.40 μmoles/kg per minute. The glycerol space was 58.1% of body weight. The relationship of glycerol concentration to rate of glycerol utilization in the intact rabbit suggests the existence of an enzyme with a KM for glycerol of 0.33 × 10−3 M; the glycerol kinase of rabbit liver was found to have a KM for glycerol of 0.29 × 10−3 M. This enzyme could account for the disappearance of glycerol in the intact animal except that its Vmax is only 4% of that expected. Possible reasons for this are discussed. A glycerol dehydrogenase with a Vmax similar to that of the glycerol kinase also exists in rabbit liver; its KM for glycerol is so high (0.5 M) that it is unlikely to play a significant role in glycerol metabolism in the normal rabbit.

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Design of a cytochrome P450BM3 reaction system linked by two-step cofactor regeneration catalyzed by a soluble transhydrogenase and glycerol dehydrogenase

Biotechnology Progress ◽

10.1002/btpr.231 ◽

2009 ◽

Vol 25 (5) ◽

pp. 1372-1378 ◽

Cited By ~ 17

Author(s):

Tsuyoshi Mouri ◽

Takeshi Shimizu ◽

Noriho Kamiya ◽

Masahiro Goto ◽

Hirofumi Ichinose

Keyword(s):

Reaction System ◽

Cofactor Regeneration ◽

Glycerol Dehydrogenase

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Design and electrical characteristic evaluation for interface circuit in isdn bus wiring system

Electronics and Communications in Japan (Part I Communications) ◽

10.1002/ecja.4410731202 ◽

1990 ◽

Vol 73 (12) ◽

pp. 9-20

Author(s):

Shizuo Nakano ◽

Naofumi Nagai

Keyword(s):

Electrical Characteristic ◽

Interface Circuit ◽

Wiring System

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Automated enzymic determination of glycerol in beverages by an immobilized glycerol dehydrogenase nylon-tube reactor

European Food Research and Technology ◽

10.1007/bf01907238 ◽

1980 ◽

Vol 171 (6) ◽

pp. 449-450 ◽

Cited By ~ 4

Author(s):

Wilhelm Hinsch ◽

Andreas Antonijevic ◽

V. Sundaram

Keyword(s):

Glycerol Dehydrogenase ◽

Tube Reactor ◽

Nylon Tube

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Structure of glycerol dehydrogenase fromSerratia

Acta Crystallographica Section F Structural Biology Communications ◽

10.1107/s2053230x13034444 ◽

2014 ◽

Vol 70 (2) ◽

pp. 166-172 ◽

Cited By ~ 5

Author(s):

Paul Musille ◽

Eric Ortlund

Keyword(s):

Protein Expression ◽

Structure Determination ◽

Gel Filtration ◽

Protein Composition ◽

Glycerol Dehydrogenase ◽

Metabolic Enzyme ◽

X Ray ◽

Unknown Protein ◽

Crystallization Experiment ◽

Additional Protein

The 1.90 Å resolution X-ray crystal structure of glycerol dehydrogenase derived from contaminating bacteria present during routineEscherichia coliprotein expression is presented. This off-target enzyme showed intrinsic affinity for Ni2+-Sepharose, migrated at the expected molecular mass for the target protein during gel filtration and was crystallized before it was realised that contamination had occurred. In this study, it is shown that liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) can efficiently identify the protein composition of crystals in a crystallization experiment as part of a structure-determination pipeline for an unknown protein. The high-resolution X-ray data enabled sequencing directly from the electron-density maps, allowing the source of contamination to be placed within theSerratiagenus. Incorporating additional protein-identity checks, such as tandem LC-MS/MS, earlier in the protein expression, purification and crystallization workflow may have prevented the unintentional structure determination of this metabolic enzyme, which represents the first enterobacterial glycerol dehydrogenase reported to date.

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