Wyniki wyszukiwania

1

A rapid method of agarose gel electrophoresis for separation of different conformational forms of DNA

100%

Ciesielska E., Szmigiero L.

Cellular and Molecular Biology Letters

|

1996

|

tom 01

|

nr 4

A fast two step method of agarose gel electrophoresis for separation of different conformational forms of DNA is described. In the first step the gel is run in the buffer without ethidium bromide and then the gel is stained with that dye. After staining the second step of electrophoresis is performed in the buffer without ethidium bromide. This two step procedure allows one to receive very good resolution between bands corresponding to relaxed, supercoiled, open circular, and linear forms of DNA.

2

An organic solvent and surfactant stable alpha-amylase from soybean seeds

72%

Jaiswal N., Prakash O.

Acta Biochimica Polonica

|

2013

|

tom 60

|

nr 3

An organic solvent and surfactant stable α-amylase was obtained from soybean seeds. The direct and indirect effect of various organic solvents (non-polar, polar protic, and polar aprotic) and surfactants on the activity and stability of free enzyme was determined. The enzyme showed a very high catalytic efficiency and stabilization against most of the organic solvents and surfactants tested, except for few. Those organic solvents and surfactants (like chloroform, dimethyl formamide, n-butanol, and Tween 20), which caused an inhibition in enzyme activity, were used to study their effects on immobilized enzyme. The inhibitory effect was found to be decreased in immobilized enzyme as compared to free enzyme indicating that immobilization imparted stability to the enzyme. Moreover, the possibility of reuse of the enzyme in the presence of the organic solvents and surfactants was increased upon immobilization. The stability of soybean α-amylase towards organic solvents and surfactants shows that it is a potential candidate for use in organic-solvent biocatalysis as well as in detergent industries.

3

Purification of the Ca2 -ATPase from rat cortical, cerebellar and hippocampal synaptosomal membranes by two - step chromatography

58%

Zylinska L., Lachowicz L., Gromadzinska E.

Cellular and Molecular Biology Letters

|

1998

|

tom 03

|

nr 1

Ca2+-ATPase, the enzyme responsible for maintenance of low resting Ca2+ level in the nerve cell, has been purified from rat cortical, cerebellar and hippocampal synaptosomal membranes by affinity chromatography on Calmodulin-Agarose which followed Reactive Red 120-Agarose column. The enzymes from these three regions ran as broad, monomeric bands on SDS-PAGE with a molecular weight at range 130-138 kDa, and were identified as a Ca2+- ATPase using monoclonal antibody 5F10. Analysis of the kinetic parameters revealed that hippocampal Ca2+-ATPase exhibited 2 times higher affinity for ATP, than cortical and cerebellar enzymes. The affinity for Ca2+ increased in order: cerebellum, cortex, and hippocampus. The differences in kinetic characteristics of purified enzymes, suggest that in adult rat brain the Ca2+-ATPase could be represented at a protein level by the region-dependent combination of several isoforms.

Ograniczanie wyników

2 Cellular and Molecular Biology Letters

1 Acta Biochimica Polonica

1 Ciesielska E.

1 Gromadzinska E.

1 Jaiswal N.

1 Lachowicz L.

1 Prakash O.

1 Szmigiero L.

1 Zylinska L.

1 2013

1 1998

1 1996

A rapid method of agarose gel electrophoresis for separation of different conformational forms of DNA

An organic solvent and surfactant stable alpha-amylase from soybean seeds

Purification of the Ca2 -ATPase from rat cortical, cerebellar and hippocampal synaptosomal membranes by two - step chromatography