Characterization of Multiple Acid Phosphatases in Salt-Stressed Spinach Leaves

1987 ◽  
Vol 14 (2) ◽  
pp. 117 ◽  
Author(s):  
SM Pan
Keyword(s):  
Molecular Weight ◽  
Salt Stress ◽  
Gel Electrophoresis ◽  
Spinacia Oleracea ◽  
Acid Phosphatases ◽  
Multiple Forms ◽  
Spinacia Oleracea L ◽  
Hydroponically Grown ◽  
Spinach Leaves

Incremental salt stress brought about a clear enhancement of the activity of acid phosphatases in hydroponically grown spinach (Spinacia oleracea L.) leaves. Sephacryl S-200 chromatography of the enzyme fraction revealed multiple forms of acid phosphatases of high (300 000), intermediate (100 000), and low (35 000) molecular weight in control and salt-stressed spinach leaves. A similar zymogram of acid phosphatases, showing at least six bands in polyacrylamide disc gel electrophoresis, was observed for control and stressed leaves. However, promotive effects of incremental salt stress on the activity of acid phosphatases were more pronounced in high molecular weight acid phosphatases. Substrate specificity and differential effects of some ions on the multiple acid phosphatases were also examined for control and salt-stressed leaves.

Consequences of salt stress on conductance to CO2 diffusion, Rubisco characteristics and anatomy of spinach leaves

1998 ◽  
Vol 25 (3) ◽  
pp. 395 ◽  
Author(s):  
Sebastiano Delfine ◽  
Arturo Alvino ◽  
Massimo Zacchini ◽  
Francesco Loreto
Keyword(s):  
Salt Stress ◽  
Spinacia Oleracea ◽  
Stomatal Closure ◽  
Salt Accumulation ◽  
Bisphosphate Carboxylase ◽  
Co2 Diffusion ◽  
Spinacia Oleracea L ◽  
Mesophyll Structure ◽  
Spinach Leaves

Spinach (Spinacia oleracea L.) leaves stressed by irrigation with water containing 1% (w/v) NaCl for 20 days had low conductance to CO2 diffusion both at the stomata and in the mesophyll. Mesophyll anatomy changed in salt-stressed leaves, which could have accounted for the decreased mesophyll conductance. Ribulose- 1,5-bisphosphate carboxylase/oxygenase in vitro activity and content were not affected by up to 20 days exposure to salinity but decreased when leaves were exposed to salt stress for longer than 20 days. Salt accumulation also caused a drop of Ca and Mg which might have decreased membrane stability and chlorophyll content, respectively. Measurements of chlorophyll fluorescence indicated that the 20-day-long salt stress did not directly affect photochemistry. We conclude that salinity reduces photosynthesis primarily by reducing the diffusion of CO2 to the chloroplast, both by stomatal closure and by changes in mesophyll structure which decreases the conductance to CO2 diffusion within the leaf. The capacity for carbon metabolism is eventually reduced but that occurs after substantial decreases in the conductance to CO2 diffusion.

Isolation and Characterization of Plasminogen Activator from Pig Leucocytes

1974 ◽  
Vol 31 (01) ◽  
pp. 072-085 ◽  
Author(s):  
M Kopitar ◽  
M Stegnar ◽  
B Accetto ◽  
D Lebez
Keyword(s):  
Molecular Weight ◽  
Plasminogen Activator ◽  
Gel Electrophoresis ◽  
Gel Filtration ◽  
Ph Optimum ◽  
Isolation And Characterization ◽  
Ph Range ◽  
Inhibition Studies ◽  
Final Purification

SummaryPlasminogen activator was isolated from disrupted pig leucocytes by the aid of DEAE chromatography, gel filtration on Sephadex G-100 and final purification on CM cellulose, or by preparative gel electrophoresis.Isolated plasminogen activator corresponds No. 3 band of the starting sample of leucocyte cells (that is composed from 10 gel electrophoretic bands).pH optimum was found to be in pH range 8.0–8.5 and the highest pH stability is between pH range 5.0–8.0.Inhibition studies of isolated plasminogen activator were performed with EACA, AMCHA, PAMBA and Trasylol, using Anson and Astrup method. By Astrup method 100% inhibition was found with EACA and Trasylol and 30% with AMCHA. PAMBA gave 60% inhibition already at concentration 10–3 M/ml. Molecular weight of plasminogen activator was determined by gel filtration on Sephadex G-100. The value obtained from 4 different samples was found to be 28000–30500.

Prothrombin Metz : Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M Ribieto ◽  
J Elion ◽  
D Labie ◽  
F Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion. Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Val-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin l (Pl) and the appearance of abnormal intermediates migrating faster than Pl.

scholarly journals Purification and Characterization of Δ1-Pyrroline-5-Carboxylate Reductase Isoenzymes, Indicating Differential Distribution in Spinach (Spinacia oleracea L.) Leaves

2001 ◽  
Vol 42 (7) ◽  
pp. 742-750 ◽  
Author(s):  
Minoru Murahama ◽  
Takayuki Yoshida ◽  
Fumio Hayashi ◽  
Takuya Ichino ◽  
Yukika Sanada ◽  
...  
Keyword(s):  
Spinacia Oleracea ◽  
Purification And Characterization ◽  
Differential Distribution ◽  
Spinacia Oleracea L ◽  
Carboxylate Reductase

Purification and Characterization of a High-Molecular-Weight Insecticidal Protein Complex Produced by the Entomopathogenic BacteriumPhotorhabdus luminescens

1998 ◽  
Vol 64 (8) ◽  
pp. 3029-3035 ◽  
Author(s):  
David J. Bowen ◽  
Jerald C. Ensign
Keyword(s):  
Molecular Weight ◽  
Insecticidal Activity ◽  
Protein Complex ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Toxin ◽  
The Family ◽  
Toxin Complex

ABSTRACT Photorhabdus luminescens is a gram-negative enteric bacterium that is found in association with entomopathogenic nematodes of the family Heterorhabditidae. The nematodes infect a variety of soil-dwelling insects. Upon entering an insect host, the nematode releases P. luminescens cells from its intestinal tract, and the bacteria quickly establish a lethal septicemia. When grown in peptone broth, in the absence of the nematodes, the bacteria produce a protein toxin complex that is lethal when fed to, or injected into the hemolymph of, Manduca sexta larvae and several other insect species. The toxin purified as a protein complex which has an estimated molecular weight of 1,000,000 and contains no protease, phospholipase, or hemolytic activity and only a trace of lipase activity. The purified toxin possesses insecticidal activity whether injected or given orally. Analyses of the denatured complex by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed it to be composed of several protein subunits ranging in size from 30 to 200 kDa. The complex was further separated by native gel electrophoresis into three components, two of which retained insecticidal activity. The purified native toxin complex was found to be active in nanogram concentrations against insects representing four orders of the classInsecta.

scholarly journals Effect of three organic fertilizers treatments on sensory evaluations of baby spinach (Spinacia oleracea L.)

2021 ◽  
Vol 27 ◽  
Author(s):  
C. Parwada ◽  
V. Chigiya ◽  
W. Ngezimana ◽  
J. Chipomho
Keyword(s):  
Spinacia Oleracea ◽  
Consumer Preferences ◽  
Organic Fertilizer ◽  
Organic Fertilizers ◽  
Teachers College ◽  
Spinacia Oleracea L ◽  
Sensory Evaluations ◽  
Hedonic Scale ◽  
Major Factors ◽  
Spinach Leaves

Sources of fertilizer are one of the major factors influencing baby spinach leaf texture, sweetness, bitterness and after-taste. However, the effects of fertilizer sources on baby spinach growth performance and consumer preferences are not known. A survey was carried out at the Seke Teachers’ College (SKC) community, Zimbabwe to determine the consumer preferences on the baby spinach grown on the organic fertilizer (cattle, poultry and goat manures) as well as on control inorganic  fertilizers (7% N, 14% P, 7% K). The study used 32 females and 30 males as panellists for sensory evaluations. Organoleptic tests were performed for the baby spinach leaves using a panel of 62 testers. An interval line scale (16 cm long) was used to measure the liking for sweetness, colour, bitterness and after-taste. A 9-point hedonic scale was used to decide the overall preferences. Organoleptic tests showed significant differences (P<0.05) in appearance and taste between the inorganic and organic fertilizers used. The baby spinach leaves grown on organic fertilizers was preferred more compared to that grown on inorganic fertilizer (control). Therefore, it is recommended to use organic fertilizers in baby spinach production in order to satisfy consumer preferences.

Prothrombin Metz: Purification and Characterization of a Variant of Human Prothrombin

1979 ◽  
Author(s):  
M.J. Rabiet ◽  
J. Elion ◽  
D. Labie ◽  
F. Josso
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Factor Xa ◽  
Polyacrylamide Gel ◽  
Cleavage Pattern ◽  
Purification And Characterization ◽  
Double Immunodiffusion ◽  
The Family

For the purification of the abnormal prothrombin (Pt Metz), advantage has been taken of the existence in the family of three siblings who, being double heterozygotes for Pt Metz and a hypoprothrombinemia, have no normal Pt. Purification procedures included barium citrate adsorption and chromatography on DEAE Sephadex as for normal Pt. As opposed to some other variants (Pt Barcelona and Madrid), Pt Metz elutes as a single symetrical peak. By SDS Polyacrylamide gel electrophoresis, this material is homogeneous and appears to have the same molecular weight as normal Pt. Comigration of normal and abnormal Pt in the absence of SDS, shows a double band suggesting an abnormal charge for the variant. Pt Metz exhibits an identity reaction with the control by double immunodiffusion.Upon activation by factor Xa, Pt Metz can generate amydolytic activity on Bz-Phe-Va1-Arg-pNa (S2160), but only a very low clotting activity. Clear abnormalities are observed in the cleavage pattern of Pt Metz when monitored by SDS gel electrophoresis. The main feature are the accumulation of prethrombin 1 (P1) and the appearance of abnormal intermediates migra-ti ng faster than P1.

Cloning, Expression and Characterization of β-Glucosidase from L. Delbrueckii Subsp. Delbrueckii in Escherichia coli

2011 ◽  
Vol 301-303 ◽  
pp. 347-351
Author(s):  
Xiu Hong Zhao ◽  
Jie Zeng ◽  
Hai Yan Gao ◽  
Chang Biao Li ◽  
Chang Jiang Liu
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Prokaryotic Expression ◽  
Expression Vector ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gene Encoding ◽  
Prokaryotic Expression Vector ◽  
Strain Bl21

Gene encoding β-glucosidase was amplified through PCR by using the genome DNA extracted from L .delbrueckii subsp. delbrueckii as a template. The gene encoding β-glucosidase was inserted into a prokaryotic expression vector pET-28a(+) and expressed in E.coli strain BL21(DE3). The gene encoding β-glucosidase was of 1380bp. The nucleotide sequence of the gene encoding β-glucosidase from L. delbrueckii subsp. delbrueckii showed as high as 97.9% homology comparing with that from L. delbrueckii subsp. bulgaricus indicating that the gene encoding β-glucosidase is highly conservative. The enzyme activity was about 34U/mg and the molecular weight of β-glucosidase is about 51 kDa analyzed by SDS-polyacrylamide gel electrophoresis.

Isolation, purification, and partial characterization of type V-A hemagglutinin from Escherichia coli GV-12, O1:H-

1982 ◽  
Vol 152 (2) ◽  
pp. 757-761
Author(s):  
V L Sheladia ◽  
J P Chambers ◽  
J Guevara ◽  
D J Evans
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Amino Terminus ◽  
N Terminus ◽  
Type V

A hemagglutinin which specifically agglutinates human type A erythrocytes (mannose resistant) was isolated from the growth medium of cultures of Escherichia coli GV-12, serotype O1:H-, and purified by chromatography on Bio-Gel A-1.5 and DEAE-Sephadex A-25. The purity of the hemagglutinin was established by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoelectrophoresis. N-terminus analysis indicated that only asparagine resides on the amino terminus. The native hemagglutinin is an aggregate exhibiting a sedimentation coefficient of 9.25, which corresponds to a molecular weight of approximately 200,000. The monomeric molecular weight was found to be approximately 16,300. Amino acid analysis indicated that the hemagglutinin consists of 131 residues, corresponding to a molecular weight of 13,400.

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