Conversion of Ammonia to Glutamate by L-Glutamic Dehydrogenase, Alcohol Dehydrogenase and NAD+ Immobilized within Lipid-Polyamide Polyethyleneimine Microcapsules

1987 ◽  
pp. 189-192 ◽  
Author(s):  
Ehud Ilan ◽  
Thomas Ming Swi Chang
Keyword(s):  
Alcohol Dehydrogenase ◽  
Glutamic Dehydrogenase

SOME INTERACTIONS OF STEROIDS, PYRIDINE NUCLEOTIDES AND ENZYMES

1963 ◽  
Vol 42 (2) ◽  
pp. 233-239 ◽  
Author(s):  
Claude A. Villee
Keyword(s):  
Alcohol Dehydrogenase ◽  
Pyridine Nucleotide ◽  
Pyridine Nucleotides ◽  
Enzyme Preparations ◽  
Glutamic Dehydrogenase

ABSTRACT The rate of reduction of DPN by crystalline glutamic dehydrogenase is increased by the addition of corticosterone or progesterone at concentrations of 10−6 m or 10−8 m. The enzyme preparations were tested and found to be free of any transhydrogenase activity. No increase in rate could be demonstrated when these steroids were added to comparable systems of malic, lactic, or alcohol dehydrogenase, which transfer hydrogen to side 1 of the pyridine nucleotide, or with α-glycerophosphate or glyceraldehyde-3-phosphate dehydrogenase, which transfer hydrogen to side 2 of the pyridine nucleotide. Thionicotinamide DPN, but not TPN, 3-pyridine aldehyde DPN, deamino DPN, or 3-acetyl pyridine DPN, when substituted for DPN with glutamic dehydrogenase gave a system that responded to added steroids.

scholarly journals Measurement of Globular Protein Molecules by Electron Microscopy

1960 ◽  
Vol 7 (4) ◽  
pp. 613-618 ◽  
Author(s):  
Cecil E. Hall
Keyword(s):  
Electron Microscopy ◽  
Alcohol Dehydrogenase ◽  
Molecular Species ◽  
Spherical Shape ◽  
Virus Protein ◽  
Molecular Weights ◽  
Liver Alcohol Dehydrogenase ◽  
Deposited Metal ◽  
Glutamic Dehydrogenase ◽  
Organic Particles

A series of molecular species with approximately spherical shape and with molecular weights between 35,000 and 250,000 were shadowed with platinum while resting on a cleaved mica surface. They were backed, stripped from the surface, and examined by electron microscopy. Materials examined were: pepsin, liver alcohol dehydrogenase, yeast alcohol dehydrogenase, glutamic dehydrogenase, polyhedral virus protein (insect), fibrinogen substructure, alkaline phosphatase, and microsomal particles from Escherichia coli. Measurements were made of widths perpendicular to the shadowing direction and heights were deduced from shadow lengths. For those molecular species with well established molecular weights the average heights correlate very well with the diameter of the theoretical sphere but the average widths are too great by 50 to 80 A due to the lateral growth of the deposited metal. Although the distortion in shape of shadowed particles is relatively large, with standardized conditions for shadowing, it is possible to make allowance for the distortion and to obtain reasonably reliable estimates of the dimensions of spherical organic particles down to a molecular weight of about 35,000.

EXAFS INVESTIGATION OF THE STRUCTURAL SITE OF LIVER ALCOHOL DEHYDROGENASE

1986 ◽  
Vol 47 (C8) ◽  
pp. C8-1165-C8-1168
Author(s):  
M. ZEPPEZAUER ◽  
C. HAAS ◽  
W. MARET ◽  
C. HERMES ◽  
R. F. PETTIFER
Keyword(s):  
Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Structural Site

TGF-β enhances alcohol dependent hepatocyte damage via downregulation of alcohol dehydrogenase I

2009 ◽  
Vol 47 (01) ◽  
Author(s):  
L Ciuclan ◽  
C Stump ◽  
I Ilkavets ◽  
H Weng ◽  
MV Singer ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Hepatocyte Damage ◽  
Alcohol Dependent

TGF-β enhances alcohol dependent hepatocyte damage via downregulation of alcohol dehydrogenase I

2009 ◽  
Vol 47 (09) ◽  
Author(s):  
LI Ciuclan ◽  
S Ehnert ◽  
I Ilkavets ◽  
H Weng ◽  
H Gaitantzi ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Hepatocyte Damage ◽  
Alcohol Dependent

Atypical Alcohol Dehydrogenase in Chilean Alcohol Addicts With and Without Hepatic Damage

1970 ◽  
Vol 31 (3) ◽  
pp. 571-577 ◽  
Author(s):  
Guillermo Ugarte ◽  
María Eugenia Pino ◽  
Herbert Altschiller ◽  
Tamara Pereda
Keyword(s):  
Alcohol Dehydrogenase ◽  
Hepatic Damage

ALCOHOL DEHYDROGENASE ACTIVITY IN ISOLATED VACUOLES OF RED BEET ROOT CELLS

Tsitologiya ◽  
2018 ◽  
Vol 60 (6) ◽  
pp. 469-475
Author(s):  
O. D. Nimaeva ◽  
◽  
E. V. Pradedova ◽  
A. B. Karpova ◽  
R. K. Salyaev ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Root Cells ◽  
Beet Root ◽  
Red Beet ◽  
Alcohol Dehydrogenase Activity
Sign in / Sign up

Export Citation Format

Share Document