ACTIVATION OF SCHRADAN BY MAMMALIAN TISSUE HOMOGENATES

1956 ◽  
Vol 34 (6) ◽  
pp. 1131-1141 ◽  
Author(s):  
R. D. O'Brien

It has been confirmed that the combined microsomal and soluble fractions of liver, in the presence of magnesium, nicotinamide, and DPN, can convert schradan to a potent anticholinesterase. DPN can be replaced by TPN, but not by ATP. DPNH can replace the DPN and soluble fraction. Catalase enhances the conversion but only when DPNH or a source of it is provided. Acetone powders of microsomes, suitably fortified, are almost ineffective in converting schradan. The pH optimum of the whole schradan-converting system is 8.1. Other properties of the system are described. Certain extrahepatic tissues, especially lung, heart, and testis, can convert schradan. The livers of all species tested convert schradan. A peroxide-mediated mechanism of oxidation is proposed.

1956 ◽  
Vol 34 (1) ◽  
pp. 1131-1141 ◽  
Author(s):  
R. D. O'Brien

It has been confirmed that the combined microsomal and soluble fractions of liver, in the presence of magnesium, nicotinamide, and DPN, can convert schradan to a potent anticholinesterase. DPN can be replaced by TPN, but not by ATP. DPNH can replace the DPN and soluble fraction. Catalase enhances the conversion but only when DPNH or a source of it is provided. Acetone powders of microsomes, suitably fortified, are almost ineffective in converting schradan. The pH optimum of the whole schradan-converting system is 8.1. Other properties of the system are described. Certain extrahepatic tissues, especially lung, heart, and testis, can convert schradan. The livers of all species tested convert schradan. A peroxide-mediated mechanism of oxidation is proposed.


1969 ◽  
Vol 115 (2) ◽  
pp. 191-197 ◽  
Author(s):  
K.-M. Wang

1. The development, localization and heterogeneity of acid phosphatase and a Zn2+-activated acid phosphatase in cellular fractions of developing chick liver were studied. 2. Acid phosphatase is distributed abundantly in the particulate and soluble fractions. The soluble fraction is rich in Zn2+-activated acid phosphatase, which attains its peak activity at about 15 days of incubation. 3. The particulate acid phosphatase activity is inhibited by fluoride but not by sodium l(+)-tartrate or cysteine. On the other hand, the soluble Zn2+-activated acid phosphatase activity is inhibited by sodium l(+)-tartrate and cysteine but not by fluoride. 4. The pH optimum of these two enzymes is similar at about 5·6. 5. The soluble Zn2+-activated acid phosphatase activity appears to be thermally stabilized by the treatment with Triton X-100 or bovine serum albumin.


1975 ◽  
Vol 53 (5) ◽  
pp. 502-508 ◽  
Author(s):  
Steve L. Taylor ◽  
Al L. Tappel

Dipeptidase activity toward Arg-Phe, Arg-Gly, and Trp-Leu exhibited bimodal distribution in the lysosomal and soluble fractions of rat liver. The majority (50–70%) of the dipeptidase activity was present in the soluble fraction. Some evidence for a plasma membrane dipeptidase, which hydrolyzes Trp-Leu but not Arg-Phe or Arg-Gly, also was found. The lysosomal dipeptidase activity had a pH optimum of 6.0–7.0, and was activated by sulfhydryl reagents. Lysosomal localization for some of the dipeptidase activity was established with Triton WR-1339 fractionation and latency experiments.


1941 ◽  
Vol 14 (1) ◽  
pp. 1-14 ◽  
Author(s):  
George F. Bloomfield ◽  
Ernest Harold Farmer

Abstract Latex rubber which has been purified to the point at which it contains an insignificant amount of nitrogen can be separated by fractional dissolution in a mixture of petroleum and acetone into a series of hydrocarbon fractions of decreasing solubility and increasing molecular magnitude. All these fractions except the highest are soluble in petroleum and in benzene. Crepe rubber, on the other hand, appears invariably to contain a small, most-soluble fraction of oxygenated rubber, and a small similar quite insoluble fraction of material of high molecular weight. Between these extremes the rubber can be divided into fractions of increasing molecular weight, although, up to the present, about 70 per cent of the total rubber has appeared in a single fraction. It may be possible later, by judicious choice of another pair of solvents, to resolve this major fraction into a series of subfractions. Kemp and Peters refer to the effect of polar nonsolvents in reducing the viscosity of rubber solutions and also in assisting to bring gel rubber into solution, phenomena to which the polar molecules conceivably contribute by countering the forces of association between the rubber molecules. The present series of fractionations was conducted throughout in the presence of a polar nonsolvent (acetone), and hence may be considered to approach towards a separation of true rubber molecules as distinct from molecular aggregates. It is found, however, that, whereas the more soluble fractions of acetone-extracted crepe rubber contain small proportions of nitrogen, the least soluble fractions contain substantial proportions. Any effect which the nitrogenous material may have in assisting to link together hydrocarbon molecules to which it is attached, i. e., in contributing to the high-molecular condition of a portion of natural rubber, remains at present uncertain in character. The fractions of rubber, and especially the higher ones, show a strong tendency to become insoluble when they have once been freed from the last traces of solvent. It seems doubtful whether the decreased solubility is due to oxygen as it would require to be effective at exceedingly low concentrations.


1962 ◽  
Vol 203 (2) ◽  
pp. 323-326 ◽  
Author(s):  
Per Björntorp ◽  
Robert H. Furman

In homogenates of rat heart pronounced lipolytic activity was found which had a broad pH optimum between 7.5 and 8.5. In the presence of a high concentration of NaCl or protamine sulfate an activity peak persisted between pH 6.5 and 7. This activity was greatest when hearts from fasting animals were preincubated with epinephrine and subsequently assayed in the presence of albumin. The activity was least in heparin-incubated samples and was inhibited by NaF. When lipase activity was determined in the presence of NaF a pH optimum of 8.5 was found. This lipase required serum protein and ammonium sulfate for optimal activity and could be inhibited by high concentrations of NaCl and by protamine sulfate. The yield of this lipase was similar whether hearts were obtained from fasting or from fed rats. This lipase was considered identical with the lipoprotein lipase described by E. D. Korn. It was found only in small amounts in the medium after incubation, in the presence of heparin, of the whole heart but in greater amounts when minced or sliced heart was used. After differential centrifugation most of the activity of both lipases was found in the mitochondrial fraction and in the soluble fraction.


2007 ◽  
Vol 62 (5-6) ◽  
pp. 382-388
Author(s):  
Dana Flodrová ◽  
Mária Dzúrová ◽  
Desana Lišková ◽  
Fairouz Ait Mohand ◽  
Danica Mislovičová ◽  
...  

The presence of various enzyme forms with terminal action pattern on pectate was evaluated in a protein mixture obtained from parsley roots. Enzymes found in the soluble fraction of roots (juice) were purified to homogeneity according to SDS-PAGE, partially separated by preparative isoelectric focusing and characterized. Three forms with pH optima 3.6, 4.2 and 4.6 clearly preferred substrates with a lower degree of polymerization (oligogalacturonates) while the form with pH optimum 5.2 was a typical exopolygalacturonase [EC 3. 2.1.67] with relatively fast cleavage of polymeric substrate. The forms with pH optima 3.6, 4.2 and 5.2 were released from the pulp, too. The form from the pulp with pH optimum 4.6 preferred higher oligogalacturonates and was not described in plants previously. The production of individual forms in roots was compared with that produced by root cells cultivated on solid medium and in liquid one.


2002 ◽  
Vol 368 (3) ◽  
pp. 865-874 ◽  
Author(s):  
Barry K. DERHAM ◽  
John J. HARDING

The role of α-crystallin as a molecular chaperone has been shown in many in vitro studies. In the present paper, we report on the chaperone function of α-crystallin within resealed erythrocyte ghosts. Eight enzymes were individually resealed within erythrocyte ghosts and assayed at zero time and at 24h. The ghost cell suspension was separated into soluble and membrane fractions. Five of the enzymes had significantly greater enzyme activity after 24h than the control within the soluble fractions. Fructation caused a decrease in enzyme activity (relative to the control). Resealing of α-crystallin within the ghost cell alongside the enzymes protected against inactivation by fructose within the soluble fraction.


1967 ◽  
Vol 45 (9) ◽  
pp. 1393-1400 ◽  
Author(s):  
Sital Moorjani ◽  
André Lemonde

Malate dehydrogenase and malic enzyme activities in the particulate (mitochondria) and soluble fraction have been determined in relation to the larval–pupal transformation of Tribolium confusum. The malate dehydrogenase activity in the soluble fraction follows a more or less inverse trend as compared with that in the particulate fraction. The malate dehydrogenase activity in the particulate and soluble fractions of the larva is attributed to different enzymes based on their electrophoretic mobility. A sudden increase in the activity of malate dehydrogenase in the soluble fraction at the end of the larval period is attributed to release of the enzyme from mitochondria by lysis. A further comparison of the larval particulate and pupal soluble malate dehydrogenase is made on the basis of their kinetic behavior. Malic enzyme is NADP-linked, although activity was also noted with NAD. The significance of the high activity of malic enzyme and malate dehydrogenase during pupation is discussed in relation to anaerobic metabolism.


1981 ◽  
Vol 61 (2) ◽  
pp. 205-212
Author(s):  
L. R. BENJAMIN ◽  
D. B. EGLI ◽  
J. E. LEGGETT

Experiments were conducted to evaluate the effect of leaf age and shading on the movement of 14C assimilates through soybean (Glycine max (L.) Merr.) leaves. Leaves on plants at initial bloom and mid-podfill were pulse-labelled with 14CO2 for 2 min and the distribution of 14C in the leaf was followed for 24 h. Initially, 90% of the 14C activity was in the 80% ethanol-soluble fraction; this decreased rapidly, and by 7 h after labeling only 10% of the initial activity was in this fraction. The 14C in starch and perchloric-acid-soluble fractions increased to a maximum level (approx. 30% of initial activity) 30 min after labeling and declined slowly over the rest of the period. After 24 h, approximately 80% of the 14C had moved out of the leaf. There was no effect of leaf age on the pattern of movement of 14C through the leaf. Completely shading the plant immediately after labeling resulted in a rapid cessation (within 30 mm) of 14C movement into starch with an accompanying retention of 14C in the 80% ethanol-soluble fraction.


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