scholarly journals Nucleic acid enzymology of extremely halophilic bacteria. Halobacterium cutirubrum polynucleotide phosphorylase

1971 ◽  
Vol 121 (4) ◽  
pp. 613-620 ◽  
Author(s):  
Pearl I. Peterkin ◽  
P. S. Fitt
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Nucleic Acid ◽  
Halophilic Bacteria ◽  
High Ionic Strength ◽  
Low Molecular Weight ◽  
Polynucleotide Phosphorylase

1. Polynucleotide phosphorylase was purified 200-fold from Halobacterium cutirubrum. 2. It is membrane-associated and can be solubilized by sonication. 3. The purified enzyme requires a high ionic strength for both stability and activity. 4. It is Mn2+-dependent, has all three typical polynucleotide phosphorylase activities and is specific for nucleoside diphosphates. 5. The enzyme is of low molecular weight.

Dissociation of Factor VIII in the Presence of Proteolytic Inhibitors

1978 ◽  
Vol 40 (02) ◽  
pp. 316-325 ◽  
Author(s):  
Ira I Sussman ◽  
Harvey J Weiss
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Factor Viii ◽  
Direct Evidence ◽  
Gel Filtration ◽  
High Ionic Strength ◽  
Procoagulant Activity ◽  
Low Molecular Weight ◽  
Bean Trypsin Inhibitor ◽  
Benzamidine Hydrochloride

SummaryWhen gel filtration of factor VIII is performed with buffers of high ionic strength (1.0 M NaCl or 0.25 M CaCl2), the procoagulant activity elutes with proteins of relatively low molecular weight. It has been suggested that in the presence of proteolytic inhibitors, the procoagulant activity would appear at the void volume. To test this hypothesis, chromatography with buffers of high ionic strength was performed in the presence of benzamidine hydrochloride, soy bean trypsin inhibitor, heparin, DFP, and aprotinin. Under all of these conditions, the procoagulant activity continued to elute with proteins of low molecular weight. Similar findings were obtained after chromatographing cryoprecipitate prepared from the plasma of a normal subject who had received heparin. Thus, at present there is no direct evidence to suggest that proteolysis is involved in the dissociation of factor VIII by buffers of high ionic strength.

scholarly journals Effect of kinetin on nucleic acid synthesis in senescing and young leaves in Brassica oleracea L. var. gongylodes L.

2015 ◽  
Vol 44 (4) ◽  
pp. 553-565
Author(s):  
J. Legocka ◽  
A. Szweykowska
Keyword(s):  
Molecular Weight ◽  
Nucleic Acid ◽  
Acid Synthesis ◽  
Inhibitory Effect ◽  
Rrna Synthesis ◽  
Low Molecular Weight ◽  
Chlorophyll B ◽  
Mature Leaves ◽  
Young Leaves ◽  
Brassica Oleracea L

In detached kohlrabi leaves senescing in the dark, the decrease in chlorophyll to was more pronounced than in chlorophyll a. The retardation by kinetin of the chlorophyll loss was also markedly stronger in the case of chlorophyll b. Using the fractionation of nucleic acids on polyacrylamide gels it has been shown that during leaf senescence the level of all RNA species decreased, whereas the amount of DNA was more or less constant. In the presence of kinetin, the loss of RNA was inhibited and the incorporation of precursor into the cytoplasmic rRNA as well as into low molecular weight RNA species was supported. Chloroplast rRNA synthesis has not been detected in mature leaves and kinetin showed no effect in this respect. In young expanding leaves detached and kept in light, the synthesis of cytoplasmic rRNA was strongly stimulated by kinetin, whereas in the case of Chloroplast rRNA only an inhibitory effect of kinetin could be found. The results suggest that the cytokinins are primarily involved in processes of the synthesis of cytoplasmic rRNA and low molecular RNA fractions, and in this way affect the development of plastids, in particular the course of their senescence.

Direct Isolation of High-Quality Low Molecular Weight RNA of Pear Peel from the Extraction Mixture Containing Nucleic Acid

2009 ◽  
Vol 44 (1) ◽  
pp. 61-65 ◽  
Author(s):  
Xin-wei Wang ◽  
Ai-sheng Xiong ◽  
Quan-hong Yao ◽  
Zhen Zhang ◽  
Yu-shan Qiao
Keyword(s):  
Molecular Weight ◽  
Nucleic Acid ◽  
Low Molecular Weight ◽  
High Quality ◽  
Extraction Mixture

scholarly journals Rabbit factor VIII: identification of size heterogeneity

Blood ◽  
1977 ◽  
Vol 49 (2) ◽  
pp. 209-217
Author(s):  
ME Rick ◽  
DE Wampler ◽  
LW Hoyer
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Factor Viii ◽  
Low Molecular Weight ◽  
Gel Chromatography ◽  
Weight Factor ◽  
Rabbit Plasma ◽  
Factor Viii Activity ◽  
Size Heterogeneity ◽  
Two Peaks

Two forms of rabbit factor VIII procoagulant activity, distinguishable by size on gel filtration and ultracentrifugation, have been identified in normal rabbit plasma. These studies have been carried out with citrate-anticoagulated rabbit plasma obtained by cardiac puncture. Two peaks of factor VIII activity were obtained on agarose gel chromatography, using physiologic ionic strength buffers: a high molecular weight peak eluting at the void volume and a second peak eluting with smaller plasma proteins. The presence of high and low molecular weight factor VIII activities was confirmed by sucrose density gradient centrifugation. The two peaks of factor VIII activity remained distinct when proteolytic inhibitors were added to the plasma and eluting buffers. Both the high and low molecular weight factor VIII procoagulant activities were inhibited by antibodies to human and rabbit factor VIII, and both were activated by thrombin. The identification of size heterogeneity of factor VIII in normal rabbit plasma, in the absence of any modification by ionic strength, may permit more satisfactory study of the relationship of factor VIII size to function.

scholarly journals Nucleic acid enzymology of extremely halophilic bacteria. Halobacterium cutirubrum ribonucleic acid-dependent ribonucleic acid polymerase

1971 ◽  
Vol 121 (4) ◽  
pp. 629-633 ◽  
Author(s):  
B. Gregory Louis ◽  
P. S. Fitt
Keyword(s):  
Molecular Weight ◽  
Sodium Chloride ◽  
Nucleic Acid ◽  
Ribonucleic Acid ◽  
Halophilic Bacteria ◽  
Chloride Concentration ◽  
Nucleoside Triphosphate ◽  
Extreme Halophile ◽  
Sodium Chloride Concentration ◽  
The Stability

1. Crude extracts of the extreme halophile Halobacterium cutirubrum contain separable DNA-dependent and RNA-dependent RNA polymerases. 2. The RNA-dependent enzyme has been purified about 2800-fold. 3. It requires RNA, preferably of high molecular weight, and all four ribonucleoside triphosphates to incorporate 14C-labelled nucleoside triphosphate into an acid-insoluble, ribonuclease-sensitive product. 4. Both the stability and activity of the RNA polymerase are relatively insensitive to changes in potassium chloride or sodium chloride concentration, but incorporation is stimulated by both Mg2+ and Mn2+. 5. The molecular weight of the enzyme is about 17000–18000.

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