Polyacrylamide Gel Synthesis of BaTiO<SUB>3</SUB> Nanoparticles and Its Photocatalytic Properties for Methyl Red Degradation

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

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Tuning the pore structures and photocatalytic properties of a 2D covalent organic framework with multi-branched photoactive moieties

Nanoscale ◽

10.1039/d0nr02994g ◽

2020 ◽

Vol 12 (30) ◽

pp. 16136-16142

Author(s):

Xuan Wang ◽

Ming-Jie Dong ◽

Chuan-De Wu

Keyword(s):

Photocatalytic Properties ◽

Effective Strategy ◽

Covalent Organic Framework ◽

Highly Efficient ◽

Pore Structures ◽

Local Connection ◽

Organic Framework

An effective strategy to incorporate accessible metalloporphyrin photoactive sites into 2D COFs by establishing a 3D local connection for highly efficient photocatalysis was developed.

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Analysis of proteins copurifying with the cd4/lck complex using one-dimensional polyacrylamide gel electrophoresis and mass spectrometry: comparison with affinity-tag based protein detection and evaluation of different solubilization methods

Journal of the American Society for Mass Spectrometry ◽

10.1016/s1044-0305(03)00895-x ◽

2004 ◽

Author(s):

O Bernhard

Keyword(s):

Mass Spectrometry ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Protein Detection ◽

Polyacrylamide Gel ◽

Affinity Tag ◽

One Dimensional

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Fabrication and photocatalytic performance of Bi 24 O 31 Br 10 nanosphere by a polyacrylamide gel method

Micro & Nano Letters ◽

10.1049/mnl.2020.0016 ◽

2020 ◽

Vol 15 (8) ◽

pp. 499-502 ◽

Cited By ~ 2

Author(s):

Zuming He ◽

Jiangbin Su ◽

Yongmei Xia ◽

Bin Tang

Keyword(s):

Photocatalytic Performance ◽

Polyacrylamide Gel ◽

Gel Method ◽

Polyacrylamide Gel Method ◽

O 31

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The Effect of Antithrombin III on the Activity of the Coagulation Factors VII, IX and X

Thrombosis and Haemostasis ◽

10.1055/s-0038-1647922 ◽

1976 ◽

Vol 35 (02) ◽

pp. 295-304 ◽

Cited By ~ 49

Author(s):

B Østerud ◽

M Miller-Andersson ◽

U Abildgaard ◽

H Prydz

Keyword(s):

Antithrombin Iii ◽

Factor Xa ◽

Coagulation Factors ◽

Disc Electrophoresis ◽

Polyacrylamide Gel ◽

Factor Vii ◽

Native Form ◽

Factor Ixa ◽

Plasma Factor

SummaryAntithrombin III, purified to homogeneity according to Polyacrylamide gel disc electrophoresis and immunoelectrophoresis, inhibited the activity of purified factor IXa and Xa, whereas factor VII was not inhibited either in the active or in the native form.Antithrombin III is the single most important inhibitor of factor Xa in plasma. Factor Xa does not, however, reduce the activity of antithrombin III against thrombin.

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