Difference in Electrophoretic Pattern of the Rice Dwarf Virus Genome Segments in Agarose and Polyacrylamide Gel Electrophoresis.

Intercellular fluid b proteins from hypersensitive Nicotiana tabacum L. cv. Xanthi-nc and N. sylvestris Speg. and Comes infected with tobacco mosaic virus were compared by two-dimensional (2-D) polyacrylamide gel electrophoresis. Except for missing bands b2, b6a, b6b, and b7b, the overall 2-D electrophoretic pattern of N. sylvestris intercellular fluid proteins was similar to the one observed with 'Xanthi-nc' tobacco. Intercellular proteins were also studied by chromatography on con-canavalin A. Glycoproteins corresponding to b6a and b7a proteins of N. tabacum and the [Formula: see text] analog of N. sylvestris were identified. These proteins are probably peroxidase isozymes, as peroxidase activities with the same electrophoretic mobility were detected after polyacrylamide gel electrophoresis. No esterase activity was associated with any b protein band in gels. Esterase activities decreased upon virus infection, but accumulation of b proteins and peroxidase activities increased.

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Isoenzyme and protein patterns of pentose-fermenting yeasts

Canadian Journal of Microbiology ◽

10.1139/m87-179 ◽

1987 ◽

Vol 33 (11) ◽

pp. 1017-1023 ◽

Cited By ~ 6

Author(s):

Robert S. Jeng ◽

Shiyuan Yu ◽

Morris Wayman

Keyword(s):

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Electrophoretic Pattern ◽

Pichia Stipitis ◽

Culture Collection ◽

Polyacrylamide Gel ◽

The Other ◽

Two Dimensional ◽

Protein Patterns

Soluble proteins were extracted from the vegetative cells of four pentose-fermenting yeasts, Candida shehatae, Pichia stipitis, R-1, and R-2, the R strains being of uncertain taxonomy, while the other two are culture collection yeasts. Isoenzyme patterns, protein patterns, and two-dimensional polypeptide mapping of these four strains were compared by polyacrylamide gel electrophoresis. The two R strains showed great similarity in two-dimensional polypeptide mapping, the pattern of sodium dodecyl sulfate – polyacrylamide gel electrophoresis, isoelectrofocusing, and isoenzymes, and may be one species. Each of the other two yeasts had its own characteristic electrophoretic pattern. The R strains showed the presence of three alcohol dehydrogenase isoenzymes compared with one for the culture collection yeasts, as well as much higher activity of malate dehydrogenase, isocitrate dehydrogenase, glucose-6-phosphate dehydrogenase, and 6-phosphogluconate dehydrogenase, which further the formation of pyruvate and ethanol.

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Ultrastructural localization of specific nucleoprotein fractions

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100081887 ◽

1978 ◽

Vol 36 (2) ◽

pp. 204-205

Author(s):

G. L. Brown

Keyword(s):

Gel Electrophoresis ◽

Mouse Liver ◽

Polyacrylamide Gel Electrophoresis ◽

Ultrastructural Localization ◽

Polyacrylamide Gel ◽

Acid Extraction ◽

Acid Solutions ◽

Low Salt ◽

Liver Nuclei ◽

Phosphate Groups

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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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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Platelet Microtubule Subunit Proteins

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657068 ◽

1979 ◽

Vol 42 (05) ◽

pp. 1630-1633 ◽

Cited By ~ 3

Author(s):

A G Castle ◽

N Crawford

Keyword(s):

Epithelial Cells ◽

Gel Electrophoresis ◽

Blood Platelets ◽

Polyacrylamide Gel Electrophoresis ◽

Polyacrylamide Gel ◽

Lens Epithelial Cells ◽

Molecular Weights ◽

Kinetics Of ◽

Microtubular Structures

SummaryBlood platelets contain microtubule proteins (tubulin and HMWs) which can be polymerised “in vitro” to form structures which resemble the microtubules seen in the intact platelet. Platelet tubulin is composed of two non-identical subunits a and p tubulin which have molecular weights around 55,000 but can be resolved in alkaline SDS-polyacrylamide gel electrophoresis. These subunits associate as dimers with sedimentation coefficients of about 5.7 S although it is not known whether the dimer protein is a homo- or hetero-dimer. The dimer tubulin binds the anti-mitotic drug colchicine and the kinetics of this binding are similar to those reported for neurotubulins. Platelet microtubules also contain two HMW proteins which appear to be essential and integral components of the fully assembled microtubule. These proteins have molecular weights greater than 200,000 daltons. Fluorescent labelled antibodies to platelet and brain tubulins stain long filamentous microtubular structures in bovine lens epithelial cells and this pattern of staining is prevented by exposing the cells to conditions known to cause depolymerisation of cell microtubules.

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

10.1055/s-0038-1665670 ◽

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.

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Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

10.1055/s-0038-1665661 ◽

1979 ◽

Author(s):

C Cierniewski ◽

T Krajewski ◽

E Janiak

Keyword(s):

Gel Electrophoresis ◽

Functional Relationship ◽

Polyacrylamide Gel Electrophoresis ◽

Polyacrylamide Gel ◽

Functional Similarity ◽

Fractionation Method ◽

Relationship Of ◽

Fibrin Monomers ◽

Fibrinogen Molecule ◽

Cold Ethanol Fractionation

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.

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Identifikasi Daging Tikus Pada Produk Baso Dengan Metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE)

YARSI Medical Journal ◽

10.33476/jky.v26i2.394 ◽

2018 ◽

Vol 26 (2) ◽

pp. 058

Author(s):

Anna P. Roswiem ◽

Triayu Septiani

Keyword(s):

Sodium Dodecyl Sulphate ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Sodium Dodecyl ◽

Polyacrylamide Gel ◽

Sds Page

Bahan baku untuk membuat baso adalah daging hewan, pada umumnya dari daging sapi, ayam, ikan dan babi. Di beberapa daerah di Indonesia terjadi kasus baso tikus. Tujuan penelitian ini adalah menguji ada tidaknya kandungan daging tikus pada produk baso yang dijual di pasar Cempaka Putih-Kecamatan Kramat Jakarta Pusat dan di pedagang baso atau mie baso di sekitar kampus Universitas YARSI Jakarta. Daging adalah protein salah satu metode untuk mengidentifikasi protein adalah metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE). Hasil penelitian menunjukkan bahwa dari 6 sampel baso terindikasi ada 2 sampel baso dengan nomor 1 dan 5 yang dibuat dari campuran daging sapi dan tikus; ada 1 sampel baso dengan nomor 6 yang terbuat dari daging tikus; dan 2 sampel baso dengan nomor 2 dan 3 yang terbuat dari campuran sapi dan babi, dan hanya 1 sampel baso dengan nomor sampel 4 yang benar-benar terbuat dari daging sapi.

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