CHOLINE KINASE OF RAPESEED (BRASSIGA CAMPESTRIS L.)

1957 ◽  
Vol 35 (10) ◽  
pp. 853-863 ◽  
Author(s):  
T. Ramasarma ◽  
L. R. Wetter
Keyword(s):  
Calcium Phosphate ◽  
Enzyme Preparation ◽  
Brassica Campestris ◽  
Maximum Activity ◽  
Choline Kinase ◽  
Aqueous Extracts ◽  
Neutral Ph ◽  
Sulphydryl Groups

Choline kinase from aqueous extracts of Polish rapeseed (Brassica campestris L.) has been purified 25-fold by fractionation with acetone and calcium phosphate gel. The purified enzyme was relatively stable when stored frozen at neutral pH, and was active over a broad range of pH, the optimum being at about pH 8.6 – 10.0. The enzyme required Mg++ and exhibited maximum activity only when the Mg++: ATP ratio was 1:1. Phosphorylcholine, ADP, and Mn++ inhibited the activity. In addition to choline, the enzyme preparation phosphorylated dimethyl- and diethyl-aminoethanol but not ethanolamine. The choline kinase from rapeseed is similar to that from yeast except that the former does not require sulphydryl groups for activation.

CHOLINE KINASE OF RAPESEED (BRASSIGA CAMPESTRIS L.)

1957 ◽  
Vol 35 (1) ◽  
pp. 853-863
Author(s):  
T. Ramasarma ◽  
L. R. Wetter
Keyword(s):  
Calcium Phosphate ◽  
Enzyme Preparation ◽  
Brassica Campestris ◽  
Maximum Activity ◽  
Choline Kinase ◽  
Aqueous Extracts ◽  
Neutral Ph ◽  
Sulphydryl Groups

Choline kinase from aqueous extracts of Polish rapeseed (Brassica campestris L.) has been purified 25-fold by fractionation with acetone and calcium phosphate gel. The purified enzyme was relatively stable when stored frozen at neutral pH, and was active over a broad range of pH, the optimum being at about pH 8.6 – 10.0. The enzyme required Mg++ and exhibited maximum activity only when the Mg++: ATP ratio was 1:1. Phosphorylcholine, ADP, and Mn++ inhibited the activity. In addition to choline, the enzyme preparation phosphorylated dimethyl- and diethyl-aminoethanol but not ethanolamine. The choline kinase from rapeseed is similar to that from yeast except that the former does not require sulphydryl groups for activation.

Phospholipid metabolism in the molluscs. II. Activities of choline kinase, ethanolamine kinase, and CTP:phosphorylethanolamine cytidyltransferase in the mollusc Helix lactea

1970 ◽  
Vol 48 (5) ◽  
pp. 580-584 ◽  
Author(s):  
Chi-Rong Liang ◽  
M. Segura ◽  
K. P. Strickland
Keyword(s):  
Digestive Gland ◽  
High Speed ◽  
Enzyme Preparation ◽  
Phospholipid Metabolism ◽  
Maximum Activity ◽  
Supernatant Fraction ◽  
Choline Kinase ◽  
Lipid Phosphorus ◽  
Ethanolamine Kinase ◽  
High Speed Supernatant

The distribution of phospholipids in the mollusc Helix lactea was investigated. The results showed that ethanolamine and choline phosphoglycerides are the major phospholipids in this species, amounting to 49% and 26% of the total lipid phosphorus. The amount of ceramide 2-aminoethylphosphonate was 9% of the total phospholipids and this compound was the only phosphonolipid detected in this species. Ethanolamine and choline kinase activities were shown to be present in the high-speed supernatant fraction of snail digestive gland. The maximum activity of choline kinase was found to be higher than that of ethanolamine kinase in the same enzyme preparation. The enzyme CTP:phosphorylethanolamine cytidyltransferase was also demonstrated in the high-speed supernatant fraction of snail digestive gland. The enzymic reaction product was identified as CDP-ethanolamine by paper chromatography and radioautography. The enzymes phosphorylcholine cytidyltransferase and aminoethylphosphonate cytidyltransferase were not detected under the conditions employed in the phosphorylethanolamine cytidyltransferase assays.

pH-Induced dissociation of bovine casein micelles. II. Mineral solubilization and its relation to casein release

1989 ◽  
Vol 56 (5) ◽  
pp. 727-735 ◽  
Author(s):  
Douglas G. Dalgleish ◽  
Andrew J. R. Law
Keyword(s):  
Calcium Phosphate ◽  
Inorganic Phosphate ◽  
Bovine Milk ◽  
Universal Relation ◽  
Casein Micelles ◽  
Neutral Ph ◽  
Quantitative Studies ◽  
A Value ◽  
Different Types ◽  
Different Temperatures

SummaryMeasurements of the release of Ca, Mg and inorganic phosphate(Pi) from the casein micelles of bovine milk have been made, as functions of the pH, in the range 4·9–6·7, and at temperatures of 4, 20 and 30 °C. The results are in general agreement with earlier published studies in giving a value of 1·75–1·84 for the micellar Ca:Pi ratio. Mg appeared to behave similarly to Ca, although the amounts of micellar material were much smaller. The results on the acid-solvation of calcium phosphate are considered in relation to published quantitative studies of the pH-induced dissociation of the different types of caseins from the micelle, and of the micellar dissociation caused when micellar calcium phosphate is dissolved at neutral pH. It is evident from this that at present it is not possible to derive a universal relation between the dissociation of minerals and of caseins from the micelles at different temperatures and under different conditions.

scholarly journals Phytochemistry and Antimicrobial Property of Fruits of Chrysophyllum albidum against Selected Clinical Isolates

2016 ◽  
Vol 55 ◽  
pp. 44-51
Author(s):  
Samuel A. Adeleye ◽  
Chimere C. Orji ◽  
Wesley Braide ◽  
Cynthia K. Akaluka
Keyword(s):  
Staphylococcus Aureus ◽  
Cardiac Glycosides ◽  
Antimicrobial Property ◽  
Maximum Activity ◽  
Clinical Isolates ◽  
Klebsiella Pneumonia ◽  
Aqueous Extracts ◽  
Methanolic Extracts ◽  
Zones Of Inhibition ◽  
Low Activity

The antimicrobial activity of methanolic and aqueous extracts ofChrysophyllum albidumfruits was investigated against clinical isolates (Staphylococcus aureus, Escherichia coli, Klebsiella pneumonia and Candida albicans). Qualitative phytochemistry of the plant indicated that the plant contained Flavonoids, Steroids, Alkaloids, Tannin, Anthraquinone and Cardiac glycosides while Saponins were reported absent. The maximum activity of the aqueous extracts in the test isolates was observed onStaphylococcus aureus, which showed clear zones with diameters of 24.0mm, 20.0mm and 16.5mm at concentrations of 100mg/ml, 50mg/ml and 25mg/ml respectively while it had low activity onKlebsiella pneumonia,with clear zones of inhibition of 15.0mm, 12.0mm and 10.5mm at same concentrations. On the other hand, Methanolic extracts activity onStaphylococcus aureusproduced clear zones of 21.0mm, 17.5mm and 12.0mm at concentrations of 200mg/ml, 100mg/ml and 50mg/ml respectively as its best activity while the it had least observed activity onKlebsiella pneumoniawith clear zones of 14.0mm, 11.5mm and 10.5mm at same concentrations. The aqueous extracts had greater activity than the methanolic extracts at same concentrations. Therefore, the fruit of the plant can be a good source of remedy in phytomedicine.

Study on Autotoxicity of Aqueous Extracts from Different Parts of Flowering Chinese Cabbage

2013 ◽  
Vol 641-642 ◽  
pp. 962-966 ◽  
Author(s):  
Hou Cheng Liu ◽  
Shi Wei Song ◽  
Ri Yuan Chen ◽  
Guang Wen Sun
Keyword(s):  
Cell Membrane ◽  
Chlorophyll Content ◽  
Chinese Cabbage ◽  
Brassica Campestris ◽  
Cell Membrane Permeability ◽  
Aqueous Extracts ◽  
Leaf Chlorophyll ◽  
Flowering Chinese Cabbage ◽  
Stems And Leaves ◽  
Different Parts

Autotoxicity of aqueous extracts from roots, stems and leaves of flowering Chinese cabbage (Brassica campestris L. ssp. chinensis var. utilis Tsen et Lee) were studied by hydroponic in different concentrations (0.5g/L, 2g/L, 5g/L). The results showed that in solution with aqueous extracts from roots, stems and leaves, the growth of flowering Chinese cabbage were inhibited, leaf chlorophyll content declined, photosynthesis rate were affected, activities of SOD, POD and CAT were changed, MDA concentration increased, thus cell membrane permeability of flowering Chinese cabbage was damaged. The autotoxicity of aqueous extracts in flowering Chinese cabbage increased with the extracts concentration increasing.

FISH-MUSCLE PURINE AND PYRIMIDINE NUCLEOSIDE PHOSPHORYLASES

1967 ◽  
Vol 45 (3) ◽  
pp. 409-419 ◽  
Author(s):  
H. L. A. Tarr ◽  
Joan E. Roy
Keyword(s):  
Enzyme Preparation ◽  
Purine Nucleoside Phosphorylase ◽  
Deae Cellulose ◽  
Fish Muscle ◽  
Purine Nucleoside ◽  
Aqueous Extracts ◽  
Pyrimidine Nucleoside ◽  
Nucleoside Phosphorylase ◽  
Pyrimidine Nucleoside Phosphorylase ◽  
Nucleoside Phosphorylases

Three purine nucleoside phosphorylase preparations (isoenzymes) were obtained by ammonium sulfate fractionation and DEAE-cellulose chromatography of aqueous extracts of lingcod muscle. Dialysis, adsorption on alumina Cγ, and elution with 0.4 M phosphate buffer yielded further purification. The most active enzyme preparation had about 120 times the activity of initial extracts. It utilized hypoxanthine, 6-mercaptopurine, guanine, 8-azaguanine, xanthine, adenine, 2,6-diaminopurine and 6-methylpurine in presence of ribose 1-phosphate or deoxyribose 1-phosphate. Several substituted purines were not utilized and did not inhibit the reaction between hypoxanthine and the pentose phosphates. The Kmwith inosine as substrate was 3.2 × 10−6 M. A pyrimidine nucleoside phosphorylase, distinct from the purine nucleoside phosphorylase, occurred in the DEAE-cellulose fraction comprising one of the purine nucleoside phosphorylases. Its activity was much lower than that of the purine nucleoside phosphorylase preparations. Uridine and thymidine were the best substrates. Deoxyuridine was a poor substrate, and neither cytidine nor deoxycytidine was utilized. The equilibrium with all preparations was about 80% in favor of nucleoside formation. The purified enzymes were all destroyed by freezing.

EFFECTS OF HYDROXYLATED DERIVATIVES OF VITAMIN D3 AND OF AQUEOUS EXTRACTS OF SOLANUM MALACOXYLON ON THE ABSORPTION OF CALCIUM, PHOSPHATE, SODIUM, POTASSIUM AND WATER FROM THE JEJUNUM OF PIGS

1979 ◽  
Vol 82 (3) ◽  
pp. 417-424 ◽  
Author(s):  
J. FOX ◽  
A. D. CARE
Keyword(s):  
Vitamin D ◽  
Calcium Phosphate ◽  
Time Course ◽  
Intestinal Loop ◽  
Delayed Response ◽  
Aqueous Extracts ◽  
Sodium Potassium ◽  
Solanum Malacoxylon ◽  
Derivatives Of ◽  
Sodium And Potassium

The effects of hydroxylated derivatives of vitamin D3 and aqueous extracts of Solanum malacoxylon on the intestinal absorption of calcium, phosphate, sodium, potassium and water have been studied in unstressed vitamin D-replete pigs each of which was surgically prepared beforehand with a Thirty–Vella loop of jejunum. The addition, for six 1 h periods of perfusion, of 1,25-dihydroxycholecalciferol (1,25-(OH)2D3) or 1α-hydroxycholecalciferol at similar concentrations (3·6–3·75 pmol/ml) to the solution used to perfuse the intestinal loop caused a rapid increase in the absorption of calcium but increased the absorption of phosphate only after a delay of at least 12 h. The absorption of both calcium and phosphate reached a maximum on the day following the addition of the vitamin D derivative to the perfusate. The addition of 25-hydroxycholecalciferol (25-(OH)D3) at a concentration of 3·75 pmol/ml was without effect on absorption except for a small increase in the absorption of phosphate on the following day. However, at higher concentrations (> 250 pmol 25-(OH)D3/ml) the absorptions of calcium and phosphate were both increased rapidly. 24,25-Dihydroxycholecalciferol was without effect on absorption at the concentration tested (3·6 pmol/ml). Aqueous extracts (1%) of the leaf of S. malacoxylon showed similar effects on absorption to those of 1,25-(OH)2D3. However, there was one point of difference; the absorption of phosphate was stimulated with a similar time course to that of calcium in contrast to its delayed response to 1,25-(OH)2D3. The absorption rates of water, sodium and potassium were not consistently affected by 1,25-(OH)2D3 or S. malacoxylon. However, the major effects of these derivatives were usually seen on the day following the day of addition to the perfusate. In contrast, 25-(OH)D3 at high concentrations had a marked effect on the absorption of water, sodium and potassium on the day of addition.

Purification and some properties of uridine diphosphate N-acetylglucosamine pyrophosphorylase from Neurospora crassa

1979 ◽  
Vol 25 (12) ◽  
pp. 1381-1386 ◽  
Author(s):  
Kenji Yamamoto ◽  
Mitsuaki Moriguchi ◽  
Hiroyasu Kawai ◽  
Tatsurokuro Tochikura
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Neurospora Crassa ◽  
Isoelectric Point ◽  
Enzyme Preparation ◽  
Divalent Cations ◽  
Gel Filtration ◽  
Maximum Activity ◽  
Uridine Diphosphate ◽  
Chromatographic Techniques

Uridine diphosphate N-acetylglucosamine pyrophosphorylase (EC. 2.7.7.23) of Neurospora crassa has been purified approximately 210-fold with dithiothreitol as the stabilizing agent by use of chromatographic techniques. The enzyme preparation appeared to be homogeneous when subjected to electrophoresis. The molecular weight was estimated as approximately 37 000 by gel filtration. The enzyme had an isoelectric point around pH 4.4.Maximum activity of the enzyme was observed at pH7.5. The enzyme required Mg2+, which may be replaced by other divalent cations such as Mn2+ and Co2+ for lesser degrees of effectiveness. The enzyme was strictly specific for UDP-N-acetylglucosamine as the substrate. The estimated values of Km were 2.2 mM for UDP-N-acetylglucosamine and 5.4 mM for inorganic pyrophosphate.The enzyme activity was highly stimulated by the addition of dithiothreitol or dithioerythritol but was lost by sulfhydryl inhibitory reagents.

SOME ENZYMIC PROPERTIES OF A PARTIALLY PURIFIED AMINOACYLASE OBTAINED FROM A POLISH VARIETY OF RAPESEED (BRASSICA CAMPESTRIS L.)

1961 ◽  
Vol 39 (5) ◽  
pp. 843-853 ◽  
Author(s):  
K. Ozaki ◽  
L. R. Wetter
Keyword(s):  
Amino Acids ◽  
Calcium Phosphate ◽  
Ammonium Sulphate ◽  
Chelating Agents ◽  
Brassica Campestris ◽  
Ph Optimum ◽  
Enzyme Preparations ◽  
Metal Chelating ◽  
Hydrolysis Of ◽  
Polish Variety

Aminoacylase, which hydrolyzes N-acetyl amino acids, has been demonstrated in rapeseed. The enzyme was purified 150-fold by fractionation with ammonium sulphate and calcium phosphate gel. The purified preparation hydrolyzed N-acetyl amino acids and in addition certain dipeptides and chloracetyl-L-tyrosine. The enzyme was stable at −20 °C and had a wide pH optimum (7.2 to 8.8). Cobalt ion was found to be an activator, while sulphydryl-reacting agents such as p-chloromercuribenzoate and some metal-chelating agents inhibited the hydrolysis. The enzyme showed rigorous specificity for the L-isomer. A comparison of the ratio of activities obtained for different enzyme preparations indicates that more than one enzyme is concerned in the hydrolysis of the different substrates.

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