Folic acid compounds in romaine lettuce

1977 ◽  
Vol 55 (8) ◽  
pp. 865-868 ◽  
Author(s):  
K. K. Batra ◽  
J. R. Wagner ◽  
E. L. R. Stokstad
Keyword(s):  
Folic Acid ◽  
Specific Activity ◽  
Deae Cellulose ◽  
High Specific Activity ◽  
Microbiological Assay ◽  
Romaine Lettuce ◽  
Positive Identification

The composition of folate coenzymes in romaine lettuce was studied. Lettuce extract was purified on QAE-Sephadex A-25 and folate compounds were separated into a monoglutamate fraction and a polyglutamate fraction by chromatography on Sephadex G-15. Both the mono- and poly-glutamate fractions were resolved on DEAE-cellulose. Positive identification of DEAE peaks was made by further cochromatography with high specific activity radioactive marker folate compounds and with differential microbiological assay. The distribution of folate compounds in lettuce is as follows: 32% 5-CH3-H4PteGlu; 1% 5-CHO-H4PteGlu; 3% 5-CHO-H4PteGlu4; 9% 5-CH3-H4PteGlu4; 13% 5-CHO-H4PteGlu5; and 31% 5-CH3-H4PteGlu5.

Composition of Pteroylpolyglutamates (Conjugated Folates) in Guinea-Pig Liver and Their Formation from Folic Acid

1972 ◽  
Vol 43 (6) ◽  
pp. 799-813 ◽  
Author(s):  
R. Corrocher ◽  
B. K. Bhuyan ◽  
A. V. Hoffbrand
Keyword(s):  
Folic Acid ◽  
Guinea Pig ◽  
Lactobacillus Casei ◽  
Deae Cellulose ◽  
Microbiological Assay ◽  
Pig Liver ◽  
Ion Exchange Column ◽  
Pteroylglutamic Acid ◽  
Guinea Pig Liver ◽  
Liver Folate

1. The composition of guinea-pig liver folates and the biochemical route of formation of liver folates from injected tritium-labelled pteroylglutamic acid (folic acid) have been studied. 2. Endogenous folate was measured by microbiological assay with Lactobacillus casei and Streptococcus faecalis, with and without deconjugation of whole liver pteroylpolyglutamates (conjugated folates). Individual folate compounds were identified by microbiological assay after fractionation of liver folates by DEAE cellulose ion-exchange column chromatography. 3. Liver folate in the guinea-pig consists of about 84–87% reduced pteroylpolyglutamates with more than three glutamate moieties/molecule, about 12–15% reduced pteroyltriglutamates, about 1% reduced pteroyldiglutamates and only traces of reduced pteroylmonoglutamates. 4. About 53% of the liver folate consists of methylated derivatives. 5. Injected pteroylglutamic acid was first rapidly reduced and formylated or methylated. Glutamate moieties were then added, probably singly, to form di-, tri- and poly-glutamates. This was a relatively slow process with a hold-up at the triglutamate stage. 6. The proportion of the labelled pteroylglutamic acid in the polyglutamate form approximated to the proportion of endogenous folates in this form after 3–4 days. 7. The amount of radioactive folate in the liver increased progressively from 1 to 84 h after injection of a standard amount of radioactive pteroylglutamic acid.

scholarly journals Purification of pig synovial collagenase to high specific activity

1979 ◽  
Vol 183 (3) ◽  
pp. 647-656 ◽  
Author(s):  
T E Cawston ◽  
J A Tyler
Keyword(s):  
Tissue Culture ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Deae Cellulose ◽  
High Specific Activity ◽  
Polyacrylamide Gel ◽  
Active Enzyme ◽  
Latent Form

1. Pig synovium in tissue culture secretes a specific collagenase in a latent form. 2. The latent enzyme was concentrated by (NH4)2SO4 precipitation and activated with 4-aminophenylmercuric acetate, and the active enzyme was purified by chromatography on Ultrogel AcA44, DEAE-cellulose, heparin-Sepharose and a zinc-chelate medium to a specific activity of 53 400 units/mg. of protein. 3. The enzyme was shown to be essentially homogeneous by polyacrylamide-gel electrophoresis. 4. The purified collagenase digested collagen to give the characteristic three-quarter and one-quarter pieces.

scholarly journals Brief Report: Lack of Effect of L-Methionine Ingestion on 14CO2 Excretion from L-Histidine (Imidazole-2-14C) in Folic Acid and Vitamin B12 Deficient Humans

Blood ◽  
1970 ◽  
Vol 35 (1) ◽  
pp. 86-89 ◽  
Author(s):  
HANNES B. STAHELIN ◽  
H. S. WINCHELL ◽  
N. KUSUBOV
Keyword(s):  
Body Weight ◽  
Folic Acid ◽  
Vitamin B12 ◽  
Specific Activity ◽  
Human Subjects ◽  
Vitamin B12 Deficiency ◽  
High Specific Activity ◽  
Inhibitory Effect ◽  
B12 Deficiency ◽  
Cell Membrane Transport

Abstract Three human subjects with folic acid and one with vitamin B12 deficiency failed to show any effect of ingestion of L-methionine (400-800 µg./kg. body weight) on the production of 14CO2 from parenterally administered high specific activity L-histidine (imidazole-2-14C). It is suggested that the inhibitory effect of methionine on intestinal absorption and cell membrane transport of histidine can explain previously published effects of methionine on the oxidation of the imidazole-2 carbon atom of L-histidine and that a direct effect of methionine on histidine metabolism need not be invoked.

scholarly journals Phospholipase A2 enzyme from the venom of Egyptian honey bee Apis mellifera lamarckii with anti-platelet aggregation and anti-coagulation activities

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Doaa A. Darwish ◽  
Hassan M. M. Masoud ◽  
Mohamed M. Abdel-Monsef ◽  
Mohamed S. Helmy ◽  
Hind A. Zidan ◽  
...  
Keyword(s):  
Apis Mellifera ◽  
Platelet Aggregation ◽  
Phospholipase A2 ◽  
Honey Bee ◽  
Specific Activity ◽  
Deae Cellulose ◽  
High Specific Activity ◽  
Inhibitory Effect ◽  
Bee Venom ◽  
Very High

Abstract Background Honey bee venom contains various enzymes with wide medical and pharmaceutical applications. Results The phospholipase A2 (PLA2) has been apparently purified from the venom of Egyptian honey bee (Apis mellifera lamarckii) 8.9-fold to a very high specific activity of 6033 U/mg protein using DEAE–cellulose and Sephacryl S-300 columns. The purified bee venom PLA2 is monomeric 16 kDa protein and has isoelectric point (pI) of 5.9. The optimal activity of bee venom PLA2 was attained at pH 8 and 45 °C. Cu2+, Ni2+, Fe2+, Ca2+, and Co2+ exhibited a complete activating effect on it, while Zn2+, Mn2+, NaN3, PMSF, N-Methylmaleimide, and EDTA have inhibitory effect. Conclusions The purified bee venom PLA2 exhibited anti-platelet aggregation and anti-coagulation activities which makes it promising agent for developing novel anti-clot formation drugs in future.

Studies of Folic Acid Compounds in Nature. III. Folic Acid Compounds in Cabbage

1973 ◽  
Vol 51 (12) ◽  
pp. 1617-1623 ◽  
Author(s):  
C. Chan ◽  
Y. S. Shin ◽  
E. L. R. Stokstad
Keyword(s):  
Folic Acid ◽  
Glutamic Acid ◽  
Specific Radioactivity ◽  
Deae Cellulose ◽  
Microbiological Assay ◽  
High Specific Radioactivity ◽  
Methyl Derivatives

The folate pattern in cabbage was studied by chromatography on Sephadex G-25 and DEAE-cellulose columns associated with markers of high specific radioactivity and with differential microbiological assay. More than 90% of cabbage folate is polyglutamates containing more than five glutamic acid residues, mainly as the 5-methyl derivatives. The distribution is as follows: 52% of total cabbage folate is 5-CH3-H4PteGlu7, 32% is 5-CH3-H4PteGluc6, 7% is 5-CH3-H4PteGlu8, 4% is 5-CHO-H4PteGlu7, and the rest is 5-CH3-H4PteGlu3–5.

scholarly journals PRODUCTION, PURIFICATION AND INHIBITION OF ALGINATE LY-ASE FROM LOCAL ISOLATE OF PSEUDOMONAS AERUGINOSA NA11

2020 ◽  
Vol 51 (6) ◽  
pp. 1726-1739
Author(s):  
R. W. Younis
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Antioxidant Activity ◽  
Incubation Temperature ◽  
Specific Activity ◽  
Radical Scavenging ◽  
Deae Cellulose ◽  
High Specific Activity ◽  
Alginate Lyase ◽  
Maximum Efficiency ◽  
Local Isolate

The point of this study was for determine of the optimum conditions and purification of alginate lyase from local isolate of Pseudomonas aeruginosa NA11, and inhibition of enzyme by various plant extracts. Forty local  isolate s of pathogenic Pseudomonas aeruginosa were screened for their ability to produce alginate lyase. Local isolate of P.aeruginosa NA11 showed the maximum efficiency for produce of alginate lyase with high specific activity (14.4 U/mg). Several factors that influence on alginate lyase production from local isolate of P.aeruginosa NA11 were studied, these factors included the type of media, carbon source, nitrogen source, the incubation temperature, pH, and the incubation period. The highest yield of alginate lyase was obtained with the A medium supplemented with 0.5 % of glucose and sodium nitrate at pH 7.5 after 24 hr. incubation at 37 °C. Two chromatographic techniques were used for purification of alginate lyase after precipitation by ammonium sulphate with saturated ratio (0-70 %),  including, ion exchange chromatography by DEAE-cellulose and gel filtration by Sephadex G-100. The two steps gave the specific activity of 155.8 U/mg protein, the purification fold was 4.15 and enzymatic yield was 64 %. The molecular weight of partial purified alginate lyase was 57 KDa. The results of antioxidant activity tests for different plants extracts utilizing DPPH radical scavenging activity were showed that the saad extract has high antioxidant activity (71 %) more than other plants extracts. While the results for inhibition experiment of alginate lyase were demonstrated that saad extract was the best inhibitor with inhibition ratio of 86 %.

The Morphology of the Rat Kidney Following Folic Acid Administration

1970 ◽  
Vol 28 ◽  
pp. 200-201
Author(s):  
Aline Byrnes ◽  
Elsa E. Ramos ◽  
Minoru Suzuki ◽  
E.D. Mayfield
Keyword(s):  
Folic Acid ◽  
De Novo ◽  
Specific Activity ◽  
Rat Kidney ◽  
Present Report ◽  
Intracellular Localization ◽  
Male Rats ◽  
Renal Hypertrophy ◽  
Electron Microscopic ◽  
Biochemical Alterations

Renal hypertrophy was induced in 100 g male rats by the injection of 250 mg folic acid (FA) dissolved in 0.3 M NaHCO3/kg body weight (i.v.). Preliminary studies of the biochemical alterations in ribonucleic acid (RNA) metabolism of the renal tissue have been reported recently (1). They are: RNA content and concentration, orotic acid-c14 incorporation into RNA and acid soluble nucleotide pool, intracellular localization of the newly synthesized RNA, and the specific activity of enzymes of the de novo pyrimidine biosynthesis pathway. The present report describes the light and electron microscopic observations in these animals. For light microscopy, kidney slices were fixed in formalin, embedded, sectioned, and stained with H & E and PAS.

Effects of Heparin Oligosaccharides with High Affinity for Antithrombin III in Experimental Venous Thrombosis

1982 ◽  
Vol 47 (03) ◽  
pp. 244-248 ◽  
Author(s):  
D P Thomas ◽  
Rosemary E Merton ◽  
T W Barrowcliffe ◽  
L Thunberg ◽  
U Lindahl
Keyword(s):  
Antithrombin Iii ◽  
Specific Activity ◽  
High Specific Activity ◽  
Factor Xa ◽  
Blood Levels ◽  
Thrombin Time ◽  
High Affinity ◽  
Very High

SummaryThe in vitro and in vivo characteristics of two oligosaccharide heparin fragments have been compared to those of unfractionated mucosal heparin. A decasaccharide fragment had essentially no activity by APTT or calcium thrombin time assays in vitro, but possessed very high specific activity by anti-Factor Xa assays. When injected into rabbits at doses of up to 80 ¼g/kg, this fragment was relatively ineffective in impairing stasis thrombosis despite producing high blood levels by anti-Xa assays. A 16-18 monosaccharide fragment had even higher specific activity (almost 2000 iu/mg) by chromogenic substrate anti-Xa assay, with minimal activity by APTT. When injected in vivo, this fragment gave low blood levels by APTT, very high anti-Xa levels, and was more effective in preventing thrombosis than the decasaccharide fragment. However, in comparison with unfractionated heparin, the 16-18 monosaccharide fragment was only partially effective in preventing thrombosis, despite producing much higher blood levels by anti-Xa assays.It is concluded that the high-affinity binding of a heparin fragment to antithrombin III does not by itself impair venous thrombogenesis, and that the anti-Factor Xa activity of heparin is only a partial expression of its therapeutic potential.

Autoprothrombin C Activity from Prothrombin with Snake Venom or Trypsin

1962 ◽  
Vol 08 (03) ◽  
pp. 425-433 ◽  
Author(s):  
Ewa Marciniak ◽  
Edmond R Cole ◽  
Walter H Seegers
Keyword(s):  
Snake Venom ◽  
Thrombolytic Agent ◽  
Sodium Citrate ◽  
Specific Activity ◽  
High Specific Activity ◽  
Citrate Solution ◽  
Clotting Factors ◽  
Activation Products ◽  
Russell’S Viper ◽  
Autoprothrombin C

SummarySuitable conditions were found for the generation of autoprothrombin C from purified prothrombin with the use of Russell’s viper venom or trypsin. DEAE chromatographed prothrombin is structurally altered and has never been found to yield autoprothrombin C and also did not yield it when Russell’s viper venom or trypsin were used. Autoprothrombin C is derived from prothrombin with tissue extract thromboplastin, but not in large amounts with the intrinsic clotting factors. With the latter thrombin and autoprothrombin III are the chief activation products. Autoprothrombin III concentrates were prepared from serum and upon activation with 25% sodium citrate solution or with Russell’s viper venom large amounts of autoprothrombin C were obtained, and this was of high specific activity. Theoretically trypsin is not a thrombolytic agent, but on the contrary should lead to intravascular clotting.

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