scholarly journals Meiosis in Coprinus: characterization and activities of two forms of DNA polymerase during meiotic stages.

1982 ◽  
Vol 2 (7) ◽  
pp. 752-757 ◽  
Author(s):  
K Sakaguchi ◽  
B C Lu
Keyword(s):  
Molecular Weight ◽  
Dna Polymerase ◽  
Meiotic Prophase ◽  
Incubation Temperature ◽  
S Phase ◽  
Low Molecular Weight ◽  
Temperature Optimum ◽  
Optimal Activity ◽  
Polycytidylic Acid ◽  
Two Peaks

Two forms of DNA polymerase have been studied in the basidiomycete Coprinus. DNA polymerase from basidiocarp tissues at zygotene-pachytene stage has been purified 3,500-fold and defined as DNA polymerase b by virtue of its insensitivity to N-ethylmaleimide and by its low molecular weight (76,000). This enzyme has optimal activity at pH 7.0 to 7.5, at 200 mM KCl, and at 25 degrees C incubation temperature. It can use polycytidylic acid-oligo(dG)12-18 as template primer in addition to homodeoxypolymers. The DNA polymerase a is mainly produced in the exponentially growing mycelium. It is sensitive to N-ethylmaleimide and has a temperature optimum at 35 degrees C. At the premeiotic S phase, activities from both polymerase a and polymerase b are found in cell-free extracts. The b enzyme is the only DNA polymerase produced during meiotic prophase. Its assayable activity exhibits two peaks, one at premeiotic S stage and one at pachytene. It is possible that DNA polymerase b is responsible for pachytene repairs involved in recombination.

Meiosis in Coprinus: characterization and activities of two forms of DNA polymerase during meiotic stages

1982 ◽  
Vol 2 (7) ◽  
pp. 752-757
Author(s):  
K Sakaguchi ◽  
B C Lu
Keyword(s):  
Molecular Weight ◽  
Dna Polymerase ◽  
Meiotic Prophase ◽  
Incubation Temperature ◽  
S Phase ◽  
Low Molecular Weight ◽  
Temperature Optimum ◽  
Optimal Activity ◽  
Polycytidylic Acid ◽  
Two Peaks

Two forms of DNA polymerase have been studied in the basidiomycete Coprinus. DNA polymerase from basidiocarp tissues at zygotene-pachytene stage has been purified 3,500-fold and defined as DNA polymerase b by virtue of its insensitivity to N-ethylmaleimide and by its low molecular weight (76,000). This enzyme has optimal activity at pH 7.0 to 7.5, at 200 mM KCl, and at 25 degrees C incubation temperature. It can use polycytidylic acid-oligo(dG)12-18 as template primer in addition to homodeoxypolymers. The DNA polymerase a is mainly produced in the exponentially growing mycelium. It is sensitive to N-ethylmaleimide and has a temperature optimum at 35 degrees C. At the premeiotic S phase, activities from both polymerase a and polymerase b are found in cell-free extracts. The b enzyme is the only DNA polymerase produced during meiotic prophase. Its assayable activity exhibits two peaks, one at premeiotic S stage and one at pachytene. It is possible that DNA polymerase b is responsible for pachytene repairs involved in recombination.

Biosynthesis of the Diguanosine Nucleotides. I. Purification and Properties of an Enzyme from Yolk Platelets of Brine Shrimp Embryos

1974 ◽  
Vol 52 (3) ◽  
pp. 231-240 ◽  
Author(s):  
A. H. Warner ◽  
P. C. Beers ◽  
F. L. Huang
Keyword(s):  
Molecular Weight ◽  
Brine Shrimp ◽  
Artemia Salina ◽  
Temperature Optimum ◽  
Small Molecular Weight ◽  
Ph Optimum ◽  
Optimal Activity ◽  
Purification And Properties

An enzyme that catalyzes the synthesis of P1P4-diguanosine 5′-tetraphosphate (Gp4G) has been isolated and purified from yolk platelets of encysted embryos of the brine shrimp, Artemia salina. The enzyme GTP:GTP guanylyltransferase (Gp4G synthetase) utilizes GTP as substrate, has a pH optimum of 5.9–6.0, a temperature optimum of 40–42 °C, and requires Mg2+ and dithiothreitol for optimal activity. The synthesis of Gp4G is inhibited markedly by pyrophosphate, whereas orthophosphate has no effect on the reaction. In the presence of GDP the enzyme also catalyzes the synthesis of P1,P3-diguanosine 5′-triphosphate (Gp3G), but the rate of synthesis is low compared with Gp4G synthesis and dependent upon other small molecular weight components of yolk platelets.

scholarly journals Separation of low molecular weight rapeseed proteins by RP-HPLC-DAD – a short report

2011 ◽  
Vol 24 (No. 1) ◽  
pp. 41-44 ◽  
Author(s):  
A. Kosińska ◽  
ChavanUD ◽  
R. Amarowicz
Keyword(s):  
Molecular Weight ◽  
Sinapic Acid ◽  
Reversed Phase ◽  
Low Molecular Weight ◽  
Short Report ◽  
Uv Spectrum ◽  
Phenolic Constituents ◽  
Separation Of Proteins ◽  
Two Peaks ◽  
Low Molecular Weight Proteins

Low molecular weight proteins were extracted and isolated from rapeseed and analysed using the HPLC-DAD method. The separation of proteins and phenolic compounds was done on the reversed phase C<sub>18</sub> column with a gradient of acetonitrile in water. The chromatogram was characterised by two peaks of low molecular weight proteins with the retention times of 19.92 and 23.24 min. Additional three main peaks of phenolic constituents were recorded on the chromatogram. One of them with maximum of UV spectrum at 328 nm was identified as sinapic acid derivatives.

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 Hydrolyzed Collagen—Sources and Applications

Molecules ◽  
2019 ◽  
Vol 24 (22) ◽  
pp. 4031 ◽  
Author(s):  
Arely León-López ◽  
Alejandro Morales-Peñaloza ◽  
Víctor Manuel Martínez-Juárez ◽  
Apolonio Vargas-Torres ◽  
Dimitrios I. Zeugolis ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Functional Activity ◽  
Incubation Temperature ◽  
Alkaline Media ◽  
Low Molecular Weight ◽  
Hydrolyzed Collagen ◽  
Enzymatic Action ◽  
Different Types ◽  
Main Factors ◽  
Different Sources

Hydrolyzed collagen (HC) is a group of peptides with low molecular weight (3–6 KDa) that can be obtained by enzymatic action in acid or alkaline media at a specific incubation temperature. HC can be extracted from different sources such as bovine or porcine. These sources have presented health limitations in the last years. Recently research has shown good properties of the HC found in skin, scale, and bones from marine sources. Type and source of extraction are the main factors that affect HC properties, such as molecular weight of the peptide chain, solubility, and functional activity. HC is widely used in several industries including food, pharmaceutical, cosmetic, biomedical, and leather industries. The present review presents the different types of HC, sources of extraction, and their applications as a biomaterial.

scholarly journals DNA Polymerases in Normal and Leukemic Human Hematopoietic Cells

Blood ◽  
1974 ◽  
Vol 44 (1) ◽  
pp. 19-32 ◽  
Author(s):  
Mary Sue Coleman ◽  
John J. Hutton ◽  
F. J. Bollum
Keyword(s):  
Molecular Weight ◽  
Dna Polymerase ◽  
Peripheral Blood ◽  
Bone Marrow Cells ◽  
Dna Polymerases ◽  
Myelogenous Leukemia ◽  
Velocity Sedimentation ◽  
Low Molecular Weight ◽  
Normal Peripheral Blood ◽  
Total Dna

Abstract DNA polymerase activities were assayed in bone marrow cells and peripheral leukocytes from normal people and patients with acute myelogenous, chronic lymphocytic, and chronic myelogenous leukemia. Extracts of subcellular components were fractionated by velocity sedimentation through sucrose density gradients and assayed using activated DNA as template. Two major DNA-dependent DNA polymerases were found in human cells with molecular weights of approximately 50,000 and 200,000 daltons, respectively. The DNA polymerase of high molecular weight is located in the soluble cytoplasmic fraction and is inhibited by N-ethylmaleimide. The low molecular weight polymerase is detected in extracts of nuclei and in the soluble fraction. It is resistant to inhibition by N-ethylmaleimide. In all cell types tested, total DNA polymerase activities were much higher in cytoplasmic than in nuclear extracts. Lymphocytes purified from normal peripheral blood had three to four times as much of both the high and low molecular weight polymerase activities per cell as purified granulocytes. Leukemic myeloblasts had 10 to 20 times as much cytoplasmic DNA polymerase activity as more mature leukocytes from normal peripheral blood. In general, immature granulopoietic cells contained higher total DNA polymerase activities than more mature granulocytes, and the major increases in polymerase activities were in the high and low molecular weight cytoplasmic enzymes rather than in the nuclear enzyme.

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