scholarly journals Purification and Characterization of Urea Transporter by SDS-PAGE from the Paddy Grown in Urea Treated Soil

2013 ◽  
Vol 18 (2) ◽  
pp. 41-47
Author(s):  
MS Haque ◽  
MK Hasan
Keyword(s):  
Trypsin Inhibitor ◽  
Egg White ◽  
Urea Transport ◽  
Urea Transporter ◽  
Purification And Characterization ◽  
Treated Soil ◽  
Marker Proteins ◽  
Sds Page ◽  
New Finding

G-50 chromatography of extract of paddy plant induced by urea revealed the major three peaks F-1, F-2 and F-3 against the absorbance at 280 nm with the number of fractions. Chromatogram was also obtained from the control of extract of paddy, however, urea-induced paddy extract showed the higher absorbance than the control showing the higher protein content. F-1 fraction for both groups having the higher molecules are considered to have the urea transporter and are applied to SDS-PAGE for purification and characterization. For identification of urea transporter, a mixture of marker proteins- ?-galactosidase, BSA, egg white albumin, pepsin, trypsin inhibitor and lysozyme were used. Depending on the mobility of the sample, urea-transporter had been identified as a large band having the MW of 50.6 kDa compared to the MW of BSA. For control, SDS-PAGE shows the same band for urea-transporter but the expression was lower than the urea-treated paddy. In SDS-PAGE gel, both bands were homogenous showing the homogeneity of urea-transporter. The results demonstrate that urea application in the soil induces the expression of urea transporter which will be a new finding for the clarification of mechanism of urea transport in plants.DOI: http://dx.doi.org/10.3329/pa.v18i2.17463 Progress. Agric. 18(2): 41 - 47, 2007

Purification and characterization of an exochitinase from Bacillus thuringiensis subsp. aizawai and its action against phytopathogenic fungi

2006 ◽  
Vol 52 (7) ◽  
pp. 651-657 ◽  
Author(s):  
Luis Morales de la Vega ◽  
J Eleazar Barboza-Corona ◽  
Maria G Aguilar-Uscanga ◽  
Mario Ramírez-Lepe
Keyword(s):  
Bacillus Thuringiensis ◽  
Sodium Dodecyl ◽  
Sclerotium Rolfsii ◽  
Phytopathogenic Fungi ◽  
Purification And Characterization ◽  
Chitinolytic Enzyme ◽  
Bacillus Thuringiensis Subsp ◽  
Sds Page ◽  
Fusarium Sp

A chitinolytic enzyme from Bacillus thuringiensis subsp. aizawai has been purified and its molecular mass was estimated ca. 66 kDa by sodium dodecyl sulfate – polyacryamide gel electrophoresis (SDS–PAGE). The enzyme was able to hydrolyze chitin to chitobiosides but not carboxymethylcellulose, cellulose, pullulan, and laminarin. Optimal pH and temperature were detected at 6 and 50 °C, respectively. Stability, in the absence of substrate, was observed at temperatures less than 60 °C and pH between 5 and 8. Enzyme activity was significantly inhibited by K+ and EDTA and completely inhibited by Hg2+. Purified chitinase showed lytic activity against cell walls from six phytopathogenic fungi and inhibited the mycelial growth of both Fusarium sp. and Sclerotium rolfsii. The biocontrol efficacy of the enzyme was tested in the protection of bean seeds infested with six phytopathogenic fungi.Key words: chitinase, Bacillus thuringiensis, purification, phytopathogenic fungi.

scholarly journals Purification and characterization of cystatin from duck egg white.

1995 ◽  
Vol 42 (3) ◽  
pp. 351-356 ◽  
Author(s):  
M Warwas ◽  
J Gburek ◽  
J Osada ◽  
K Gołab
Keyword(s):  
Egg White ◽  
Amino Acid Sequences ◽  
Size Exclusion ◽  
Molecular Forms ◽  
Sds Page ◽  
Peptidase Inhibitor ◽  
Size Exclusion Hplc ◽  
Duck Egg ◽  
Chicken Cystatin

It is the second peptidase inhibitor, after ovostatin, which showing the same antipapain activity in egg white in different avian species implies differences in amino-acid sequences. Cystatin from duck egg white was purified by carboxymethylpapain affinity chromatography and size-exclusion HPLC. The purified inhibitor which showed partial identity in the immunodiffusion test with chicken egg white cystatin, had an apparent molecular mass of 9.3 kDa as determined by SDS/PAGE. IEF analysis revealed five molecular forms of pI in the range 7.8-8.4. The obtained cystatin was neither glycosylated nor phosphorylated as it is in the case of chicken cystatin. The determined Ki (0.005 +/- 0.001 nM) was similar to that reported for human and chicken cystatin C.

scholarly journals Variation of egg proteins between bird varieties by using SDS-PAGE

2019 ◽  
Vol 12 (1) ◽  
pp. 68-73
Author(s):  
Questan Amin ◽  
Hemn Zhahir ◽  
Ahmed Shaker
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Trypsin Inhibitor ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Egg Yolk ◽  
Egg White ◽  
Yolk Proteins ◽  
Egg White Proteins ◽  
Sds Page

Proteins are essential constituents of all organisms; both egg white proteins and egg yolk are source of protein. The aim of this study was conducted to perform preliminary studies to analyses and compare egg white proteins and yolk proteins from different avian species (guineafowl, dwarf hens, local hen, Shami, turkey, duck, geese, partridge and quail) via or with SDS-PAGE (Sodium Dodecyl Sulfate–Polyacrylamide Gel Electrophoresis ). 18 Fresh eggs of different poultry species (guineafowl, dwarf hens, local hen, Shami, turkey, duck, geese, partridge and quail) were collected from various farms in the Sulaimani province. Data on egg proteins were analyzed using Statistical Xlstate used for dendrogram construction and PCA. The main egg white proteins were Ovomicin, Ovotransferrin, Ovalbumin, Flavoprotein, α- chymotrypsinogen, and Trypsin inhibitor. The main lipoproteins were Apovitellenin VI, Apovitellenin Vb, Apovitellenin V, Apovitellenin IIIa, Apovitellenin III, Apovitellin 7, B-Livetin, Apovitellenin IIa, Apovitellenin II, and Apovitellenin I. All these lipoproteins were observed in the nine birds species. The egg white proteins and yolk lipoproteins for nine species were examined. It can be concluded the large differences were found in a mount of egg white proteins and yolk lipoproteins of the nine species of birds.

scholarly journals Purification and Characterization of a Trypsin Inhibitor from Lily Buld (Lilium lancifolium).

1998 ◽  
Vol 45 (11) ◽  
pp. 663-670 ◽  
Author(s):  
Toshio ASAO ◽  
Miwa HORIGUCHI ◽  
Chikako TERADA ◽  
Kyoko TAKAHASHI
Keyword(s):  
Trypsin Inhibitor ◽  
Purification And Characterization ◽  
Lilium Lancifolium

scholarly journals Purification and Characterization of a Novel Kazal-Type Trypsin Inhibitor from the Leech of Hirudinaria manillensis

Toxins ◽  
2016 ◽  
Vol 8 (8) ◽  
pp. 229 ◽  
Author(s):  
Yanmei Lai ◽  
Bowen Li ◽  
Weihui Liu ◽  
Gan Wang ◽  
Canwei Du ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Purification And Characterization

Purification and Characterization of Cytochrome c6 from the Unicellular Green Alga Scenedesmus obliquus

1997 ◽  
Vol 52 (11-12) ◽  
pp. 740-746 ◽  
Author(s):  
Röbbe Wünschiers ◽  
Thomas Zinn ◽  
Dietmar Linder ◽  
Rüdiger Schulz
Keyword(s):  
Cytochrome C ◽  
Green Alga ◽  
Scenedesmus Obliquus ◽  
Terminal Sequence ◽  
Ammonium Sulfate Precipitation ◽  
Purification And Characterization ◽  
Unicellular Green Alga ◽  
Sds Page ◽  
Monoraphidium Braunii

Abstract Purification of a soluble cytochrome c6 from the unicellular green alga Scenedesmus obliquus by a simple and rapid method is described. The purification procedure includes ammonium sulfate precipitation and non-denaturating PAGE. The N-terminal sequence of the first 20 amino acids was determined and shows 85% similarity and 75% identity to the sequence of cytochrome c6 from the green alga Monoraphidium braunii. The ferrocyto-chrome shows typical UV/VIS absorption peaks at 552.9, 521.9 and 415.7 nm. The apparent molecular mass was estimated to be 12 kD a by SDS-PAGE. EPR-spectroscopy at 20K shows resonances indicative for two distinct low-spin heme forms.

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