Radioactive Diisopropyl Fluorophosphate

1948 ◽  
Vol 70 (11) ◽  
pp. 3886-3887 ◽  
Author(s):  
Benjamin Witten ◽  
Jacob I. Miller
Keyword(s):  
Diisopropyl Fluorophosphate

Plasminogen-Activator in Human Early Milk: Its Partial Purification and Characterization

1981 ◽  
Vol 45 (02) ◽  
pp. 121-126 ◽  
Author(s):  
Utako Okamoto ◽  
Noboru Horie ◽  
Yoko Nagamatsu ◽  
Jun-Ichiro Yamamoto
Keyword(s):  
Plasminogen Activator ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Partial Purification ◽  
Order Kinetic ◽  
Diisopropyl Fluorophosphate ◽  
Step Procedure ◽  
Activity Band ◽  
C 50 ◽  
Gel Isoelectric Focusing

SummaryMilk plasminogen-activator was partially purified from human transitional milk collected at about 10 days after delivery, by a five-step procedure involving chloroform treatment, ammonium sulfate precipitation, and column chromatography on Sephadex G-150, CM Sephadex C-50 and DEAE Sephadex A-50. This gave milk-activator with a maximum purification factor of about 2,400-fold with respect to the skimmed milk. The CM Sephadex-step preparation showed, on polyacrylamide gel electrophoresis, a single plasminogen-activator activity band located between the bands of albumin and prealbumin of human serum. This preparation exhibited no kinin forming activity. The activator hydrolyzed acetyl-glycyl-L-lysine methyl ester with similar order kinetic constants to urokinase, and was inhibited strongly by diisopropyl-fluorophosphate. The molecular weight of the activator as estimated by gel filtration was approximately 86,000, the isoelectric points as estimated by gel isoelectric focusing were pH 7.2, 6.9 and 6.6, and the activator activity was not quenched by antiurokinase globulin, indicating that the milk-activator is a different entity from urokinase.

scholarly journals THE pH DEPENDENCE AND DISSOCIATION CONSTANTS OF ESTERASES AND PROTEASES TREATED WITH DIISOPROPYL FLUOROPHOSPHATE

1957 ◽  
Vol 226 (2) ◽  
pp. 867-872 ◽  
Author(s):  
L.A. Mounter ◽  
H.C. Alexander ◽  
Kenneth D. Tuck ◽  
Lien Tien H. Dien
Keyword(s):  
Dissociation Constants ◽  
Ph Dependence ◽  
Diisopropyl Fluorophosphate

scholarly journals APPARENT SPECIFIC INHIBITION OF PLANT ACETYLESTERASE BY DIISOPROPYL FLUOROPHOSPHATE

1947 ◽  
Vol 170 (1) ◽  
pp. 417-418
Author(s):  
E.F. Jansen ◽  
Marvel-Dare Fellows Nutting ◽  
A.K. Balls
Keyword(s):  
Specific Inhibition ◽  
Diisopropyl Fluorophosphate

scholarly journals Binding of 125I-fasciculin to rat brain acetylcholinesterase. The complex still binds diisopropyl fluorophosphate

1993 ◽  
Vol 268 (17) ◽  
pp. 12458-12467
Author(s):  
P. Marchot ◽  
A. Khélif ◽  
Y.H. Ji ◽  
P. Mansuelle ◽  
P.E. Bougis
Keyword(s):  
Rat Brain ◽  
Diisopropyl Fluorophosphate ◽  
Brain Acetylcholinesterase

Acetylsalicylic acid hydrolase of gastric mucosa.

1978 ◽  
Vol 234 (6) ◽  
pp. E606
Author(s):  
J G Spenney
Keyword(s):  
Gastric Mucosa ◽  
Enzymatic Activity ◽  
Acetylsalicylic Acid ◽  
Sodium Dodecyl ◽  
Sodium Cholate ◽  
Acid Hydrolase ◽  
Sulfhydryl Reagents ◽  
Ph Optimum ◽  
Diisopropyl Fluorophosphate

Acetylsalicylic acid hydrolase activity of rabbit fundic gastric mucosa has been isolated from the soluble 100,000 X g supernate. The enzymatic activity was partially purified by ammonium sulfate precipitation. The Km for acetylsalicylate was 2 mM and pH optimum was 8.6. The activity was insensitive to ionic strength, slightly inhibited by inclusion of 100 mM Cl-, and demonstrated no requirement for Ca2+ or Mg2+. Acetylsalicylic acid esterase was markedly inhibited by sodium cholate and sodium dodecyl sulfate. The enzyme was insensitive to sulfhydryl reagents with the exception of p-chloromercuribenzenesulfonic acid, which markedly inhibited the enzyme. Diisopropyl fluorophosphate (DFP) inhibited enzymatic activity with a Ki of 9 X 10(-9)M. Eserine was also inhibitory with a Ki of 0.25 mM. Inhibition by DFP at low concentration and by eserine at millimolar concentrations suggests that this enzyme is related to the group of aliphatic esterases. Identification of potent inhibitors will enable studies to define the role of this enzyme with the use of experimental preparations in which systemic toxicity can be avoided.

Acute effects of diisopropyl fluorophosphate (DFP) on autonomic and behavioral thermoregulatory responses in the Long-Evans rat

Toxicology ◽  
1991 ◽  
Vol 67 (1) ◽  
pp. 1-14 ◽  
Author(s):  
Christopher J. Gordon ◽  
Lela Fogelson ◽  
Lydia Lee ◽  
Jerry Highfill
Keyword(s):  
Acute Effects ◽  
Diisopropyl Fluorophosphate ◽  
Thermoregulatory Responses ◽  
Long Evans

scholarly journals Association of a protease with polytene chromosomes of Drosophila melanogaster.

1980 ◽  
Vol 87 (2) ◽  
pp. 415-419 ◽  
Author(s):  
J Cavagnaro ◽  
D A Pierce ◽  
J C Lucchesi ◽  
C B Chae
Keyword(s):  
Acetic Acid ◽  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Protease Inhibitors ◽  
Polytene Chromosomes ◽  
Fixation Procedure ◽  
Apparent Effect ◽  
Chloromethyl Ketone ◽  
Diisopropyl Fluorophosphate ◽  
Uniform Labeling

Incubation of Drosophila salivary glands with radioactive diisopropyl fluorophosphate results in the uniform labeling of polytene chromosomes. Extensive labeling is seen only when chromosome squashes are prepared by a formaldehyde fixation procedure and not by standard acetic acid techniques. The labeling is inhibited in the presence of tosylphenylalanine chloromethyl ketone and phenylmethane sulfonylfluoride but not by tosyllysine chloromethyl ketone, suggesting that a chymotrypsin-like serine protease is associated with the chromosomes. Protease inhibitors show no apparent effect on heat-shock specific puffing.

Sinapine Esterase I. Characterization of Sinapine Esterase from Cotyledons of Raphanus sativus

1979 ◽  
Vol 34 (9-10) ◽  
pp. 715-720 ◽  
Author(s):  
Gerhild Nurmann ◽  
Dieter Strack
Keyword(s):  
Enzyme Activity ◽  
Esterase Activity ◽  
Raphanus Sativus ◽  
Sinapic Acid ◽  
Inhibitory Effect ◽  
Ph Optimum ◽  
Diisopropyl Fluorophosphate ◽  
E 600 ◽  
Red Radish

Abstract From cotyledons of Raphanus sativus (red radish) an esterase activity which catalyzes the hy­drolysis of sinapine into sinapic acid and choline has been isolated. The enzyme, which has a near absolute specificity, is not analogous with any esterase described in the literature. The reaction has a pH optimum of 8.5 and the apparent Km is 1.95 × 10-5 m. The enzyme is relatively insensi­tive to both physostigmine (eserine) {Ki = 1.73 × 10-4 m) and neostigmine (Ki = 2 .1 3 × 10-4 ᴍ). Diisopropyl fluorophosphate (DFP) showed no inhibition and diethyl p-nitrophenylphosphate (E 600) only a slight inhibitory effect at 10-5 ᴍ, respectively. Choline (10-2 ᴍ) was inhibitory but acetylcholine (10-2 ᴍ) stimulated the enzyme activity.

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