Study of Enzyme Purification Method and Growth Pattern for Pseudomonas putida in Mercury Removal

2018 ◽  
Vol 4 (2) ◽  
Keyword(s):  
Pseudomonas Putida ◽  
Growth Pattern ◽  
Enzyme Purification ◽  
Mercury Removal ◽  
Purification Method

Development of a simplified purification method for a novel formaldehyde dismutase variant from Pseudomonas putida J3

2017 ◽  
Vol 241 ◽  
pp. 69-75 ◽  
Author(s):  
Lisa Blaschke ◽  
Wenke Wagner ◽  
Christina Werkmeister ◽  
Marion Wild ◽  
Adrian Gihring ◽  
...  
Keyword(s):  
Pseudomonas Putida ◽  
Purification Method

scholarly journals Закономірності росту фосфатмобілізувальних бактерій у різних типах живильних середовищ

2010 ◽  
Vol 1 (1) ◽  
pp. 78-82
Author(s):  
K. V. Lavrentyeva ◽  
N. V. Cherevach ◽  
A. I. Vinnikov
Keyword(s):  
Pseudomonas Putida ◽  
Growth Pattern ◽  
Physiological Parameters ◽  
Mineral Medium ◽  
Bacterial Cells ◽  
Bacteria Growth ◽  
Soil Phosphate ◽  
Constant Ph

Regularities of two strains of soil phosphate-mobilizing bacteria growth were investigated in different media. Curve of growth and physiological parameters were defined for Pseudomonas putida and Enterobacter dissolvens. Growth pattern of investigated strains was better in the broth medium than in mineral. In these conditions higher concentration of viable bacterial cells was common for E. dissolvens. It was shown that during cultivation pH of mineral medium went down to 4.4-4.5, but broth medium had constant pH 7.0.

Uultrastructure of Microtubules

1972 ◽  
Vol 30 ◽  
pp. 252-253
Author(s):  
Ariaki Nagayama
Keyword(s):  
Fine Structure ◽  
Cultured Cells ◽  
Present Report ◽  
Confluent Monolayer ◽  
Purification Method ◽  
Vinca Rosea ◽  
L Cells ◽  
Antimitotic Activity ◽  
Monolayer Cultures ◽  
Rapid Purification

Vinblastine(Vb) or vincristine, alkaloid derived from Vinca rosea is known for its antimitotic activity by regrouping of microtubules into paracrystalline form within the cells. A rapid purification method of vinblastine-induced microtubular paracrystals(PC) has provided us with a fresh and pure microtubular material demonstrating the presence of a labile ATPase associated with the PC. The present report is concerned with the fine structure of purified microtubules of mammalian cultured cells.Confluent monolayer cultures of L cells were incubated for 20hrs with 10-5 M Vb (donated from Shionogi Seiyaku & Co., Osaka, Japan).

New purification method for vitamin A derived aging pigments

Planta Medica ◽  
2010 ◽  
Vol 76 (12) ◽  
Author(s):  
E Jee ◽  
S Kim ◽  
Y Jang
Keyword(s):  
Vitamin A ◽  
Purification Method

Isolation of Human Fibrinogen and its Derivatives by Affinity Chromatography on Gly-Pro-Arg-Pro-Lys-Fractogel

1990 ◽  
Vol 63 (03) ◽  
pp. 439-444 ◽  
Author(s):  
C Kuyas ◽  
A Haeberli ◽  
P Walder ◽  
P W Straub
Keyword(s):  
Gel Electrophoresis ◽  
Affinity Purification ◽  
Polyacrylamide Gel Electrophoresis ◽  
Ease Of Use ◽  
Terminal Sequence ◽  
Purification Method ◽  
Human Fibrinogen ◽  
Isolation Methods ◽  
One Step ◽  
Complementary Binding

SummaryWith an immobilized synthetic pentapeptide GlyProArgProLys comprising the N-terminal sequence GlyProArg of the α-chain of fibrin, a new affinity method for the quantitative isolation of fibrinogen out of anticoagulated plasma was developed. The method proved to be superior to all known isolation methods in respect to ease of use and yield, since fibrinogen could be isolated in one step out of plasma with a recovery of more than 95% when compared to the immunologically measurable amounts of fibrinogen. Moreover the amounts of contaminating proteins such as fibronectin, factor XIII or plasminogen were negligible and the purity of the isolated fibrinogen was higher than 95% as measured by polyacrylamide gel electrophoresis. The clottability was 90% and more. Another advantage of this affinity purification method is the possibility to isolate fibrinogen quantitatively out of small plasma samples (<5 ml). Further, abnormal fibrinogen molecules, provided their complementary binding site for GlyProArg is preserved, may also be quantitatively isolated independent of any solubility differences as compared to normal fibrinogen. In addition fibrin(ogcn) fragments originating from plasmic digestion can be separated on the basis of their affinity to GlyProArg. The described affinity gel can be used more than 50 times without any loss of capacity.

Use of Factor VIII in the Treatment of Hemophilia

1962 ◽  
Vol 07 (02) ◽  
pp. 230-238 ◽  
Author(s):  
A Pavlovsky ◽  
H Peterson ◽  
G Casillas ◽  
C Simonetti ◽  
A Martinez Canaveri ◽  
...  
Keyword(s):  
Factor Viii ◽  
Tannic Acid ◽  
Deae Cellulose ◽  
Fibrinolytic System ◽  
Purification Method ◽  
Fraction I

SummaryThis publication describes the results obtained by treatment of haemophiliacs with factor VIII preparations isolated from Cohn fraction I by use of tannic acid, FI-O-Ta.The authors stress the rapidity of the disappearance of factor VIII after injection. Transfusions are generally well tolerated. One reaction of the pyrogen type has been observed and also a case of activation of the fibrinolytic system.A second purification method by means of chromatography on DEAE-cellulose is described.

A Novel Method for the Rapid Purification of Human and Rat Fibrin(OGEN) Degradation Products in High Yields

1979 ◽  
Author(s):  
W. Nieuwenhuizen ◽  
I. A. M. van Ruijven-Vermeer ◽  
F. Haverkate ◽  
G. Timan
Keyword(s):  
Degradation Products ◽  
Complete Separation ◽  
Purification Method ◽  
Amino Terminal ◽  
Novel Method ◽  
Rapid Purification ◽  
The One ◽  
High Yields ◽  
Size Heterogeneity ◽  
D Dimer

A novel method will be described for the preparation and purification of fibrin(ogen) degradation products in high yields. The high yields are due to two factors. on the one hand an improved preparation method in which the size heterogeneity of the degradation products D is strongly reduced by plasmin digestion at well-controlled calcium concentrations. At calcium concentrations of 2mM exclusively D fragments, M.W.= 93-000 (Dcate) were formed; in the presence of 1OmM EGTA only fragments M.W.= 80.000 (D EGTA) were formed as described. on the other hand a new purification method, which includes Sephadex G-200 filtration to purify the D:E complexes and separation of the D and E fragments by a 16 hrs. preparative isoelectric focussing. The latter step gives a complete separation of D (fragments) (pH = 6.5) and E fragments (at pH = 4.5) without any overlap, thus allowing a nearly 100% recovery in this step. The overall recoveries are around 75% of the theoretical values. These recoveries are superior to those of existing procedures. Moreover the conditions of this purification procedure are very mild and probably do not affect the native configuration of the products. Amino-terminal amino acids of human Dcate, D EGTA and D-dimer are identical i.e. val, asx and ser. in the ratgly, asx and ser were found. E 1% for rat Dcate=17-8 for rat D EGTA=16.2 and for rat D- dimer=l8.3. for the corresponding human fragments, these values were all 20.0 ± 0.2.

Sign in / Sign up

Export Citation Format

Share Document