scholarly journals Crystalline Complex of Allyl Alcohol with Copper(I) Chloride

1967 ◽  
Vol 40 (5) ◽  
pp. 1171-1174 ◽  
Author(s):  
Tetsuya Ogura ◽  
Nobuo Furuno ◽  
Shinichi Kawaguchi
Keyword(s):  
Allyl Alcohol ◽  
Crystalline Complex

Preparation and Properties of Human Prothrombin Complex

1970 ◽  
Vol 24 (03/04) ◽  
pp. 325-333 ◽  
Author(s):  
G. H Tishkoff ◽  
L. C Williams ◽  
D. M Brown
Keyword(s):  
Molecular Weight ◽  
Proteolytic Enzyme ◽  
Enzyme Inhibitor ◽  
Specific Activity ◽  
Crystalline Form ◽  
Sedimentation Equilibrium ◽  
Crystalline Complex ◽  
Interaction Product ◽  
Proteolytic Enzyme Inhibitor ◽  
Purification Scheme

SummaryAs a corollary to our previous studies with bovine prothrombin, we have initiated a study of human prothrombin complex. This product has been isolated in crystalline form as a barium glycoprotein interaction product. Product yields were reduced compared to bovine product due to the increased solubility of the barium glycoprotein interaction product. On occasion the crystalline complex exhibited good yields. The specific activity of the crystalline complex was 1851 Iowa u/mg. Further purification of human prothrombin complex was made by removal of barium and by chromatography on Sephadex G-100 gels. The final product evidenced multiple procoagulant activities (II, VII, IX and X). The monomeric molecular weight determined by sedimentation equilibrium in a solvent of 6 M guanidine-HCl and 0.5% mercaptoethanol was 70,191 ± 3,057 and was homogeneous with respect to molecular weight. This product was characterized in regard to physical constants and chemical composition. In general, the molecular properties of human prothrombin complex are very similar to the comparable bovine product. In some preparations a reversible proteolytic enzyme inhibitor (p-aminophenylarsonic acid) was employed in the ultrafiltration step of the purification scheme to inhibit protein degradation.

scholarly journals Positive Selection of Novel Peroxisome Biogenesis-Defective Mutants of the Yeast Pichia pastoris

Genetics ◽  
1999 ◽  
Vol 151 (4) ◽  
pp. 1379-1391
Author(s):  
Monique A Johnson ◽  
Hans R Waterham ◽  
Galyna P Ksheminska ◽  
Liubov R Fayura ◽  
Joan Lin Cereghino ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Allyl Alcohol ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeast ◽  
Direct Selection ◽  
Toxic Exposure ◽  
Peroxisome Biogenesis ◽  
Yeast Pichia Pastoris ◽  
Methylotrophic Yeast Pichia Pastoris ◽  
Selection Of

Abstract We have developed two novel schemes for the direct selection of peroxisome-biogenesis-defective (pex) mutants of the methylotrophic yeast Pichia pastoris. Both schemes take advantage of our observation that methanol-induced pex mutants contain little or no alcohol oxidase (AOX) activity. AOX is a peroxisomal matrix enzyme that catalyzes the first step in the methanol-utilization pathway. One scheme utilizes allyl alcohol, a compound that is not toxic to cells but is oxidized by AOX to acrolein, a compound that is toxic. Exposure of mutagenized populations of AOX-induced cells to allyl alcohol selectively kills AOX-containing cells. However, pex mutants without AOX are able to grow. The second scheme utilizes a P. pastoris strain that is defective in formaldehyde dehydrogenase (FLD), a methanol pathway enzyme required to metabolize formaldehyde, the product of AOX. AOX-induced cells of fld1 strains are sensitive to methanol because of the accumulation of formaldehyde. However, fld1 pex mutants, with little active AOX, do not efficiently oxidize methanol to formaldehyde and therefore are not sensitive to methanol. Using these selections, new pex mutant alleles in previously identified PEX genes have been isolated along with mutants in three previously unidentified PEX groups.

Toxicity of Glycols and Allyl Alcohol Evaluated by Means of Co-cultures of Microcarrier-attached Rat Hepatocytes and BALB/C 3T3 Mouse Fibroblasts

1992 ◽  
Vol 20 (2) ◽  
pp. 266-270
Author(s):  
Jens-Uwe Voss ◽  
Hasso Seibert
Keyword(s):  
Lactate Dehydrogenase ◽  
Ethylene Glycol ◽  
Allyl Alcohol ◽  
Rat Hepatocytes ◽  
3T3 Cells ◽  
Active Metabolites ◽  
Mediated Effects ◽  
Cells Cultured

The toxicity of allyl alcohol and several glycols (ethylene glycol, 1,2-propanediol, 1,3-propanediol, methoxyethanol, and the glycol ether dioxane) was studied in cultures of 3T3 cells and in co-cultures of 3T3 cells with microcarrier-attached hepatocytes. Metabolism-mediated effects on the cytotoxicity to 3T3 cells were recorded by differences in the growth of the cultures exposed in the presence or absence of hepatocytes. Hepatocyte viability was determined by depletion of intracellular lactate dehydrogenase and effects on the biotransformation ability of hepatocytes were assessed by determination of O-deethylation of 7-ethoxycoumarin (EOD activity). Allyl alcohol was the only substance more toxic to the hepatocytes than to 3T3 cells cultured in the absence of hepatocytes. Toxicity to 3T3 cells of allyl alcohol, ethylene glycol, and 1,3-propanediol, but not of 1,2-propanediol, methoxyethanol and dioxane, was markedly enhanced when the cells were co-cultured with hepatocytes. The results indicate that the toxicity of allyl alcohol, ethylene glycol, and 1,3-propanediol, to 3T3 cells depends on the formation of active metabolites. For ethylene glycol and 1,3-propanediol, growth of 3T3 cells in co-cultures was reduced at concentrations without effects on hepatocyte viability. Co-culture of 3T3 cells with microcarrier-attached rat hepatocytes represents a suitable approach for the in vitro evaluation of metabolism-mediated cytotoxicity.

Copper(I) catalyzed 2π + 2π photocycloadditions of allyl alcohol

1978 ◽  
Vol 19 (16) ◽  
pp. 1367-1370 ◽  
Author(s):  
Robert G. Salomon ◽  
Amitabha Sinha
Keyword(s):  
Allyl Alcohol

Biomimetic processes. IV. Carbocationic polymerization of isoprene initiated by dimethyl allyl alcohol

2009 ◽  
Vol 47 (8) ◽  
pp. 2181-2189 ◽  
Author(s):  
Judit E. Puskas ◽  
Clément Peres ◽  
Frédéric Peruch ◽  
Alain Deffieux ◽  
David E. Dabney ◽  
...  
Keyword(s):  
Allyl Alcohol ◽  
Carbocationic Polymerization
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