ELECTROPHORETIC DETECTION OF PARASITISM BY DRYINIDAE IN TYPHLOCYBINAE LEAFHOPPERS (HOMOPTERA: AUCHENORRHYNCHA)

1998 ◽  
Vol 130 (4) ◽  
pp. 407-414 ◽  
Author(s):  
Stefano Demichelis ◽  
Aulo Manino
Keyword(s):  
Vitis Vinifera ◽  
Gel Electrophoresis ◽  
Enzyme System ◽  
Early Stage ◽  
Polyacrylamide Gel Electrophoresis ◽  
Corylus Avellana ◽  
Polyacrylamide Gel ◽  
Glycerophosphate Dehydrogenase ◽  
Solatium Tuberosum ◽  
First Time

AbstractNine species of the subfamily Typhlocybinae (Auchenorrhyncha: Cicadellidae) were collected from Corylus avellana L., Solatium tuberosum L., and Vitis vinifera L. Seven species were parasitized by Dryinidae, among which Alebra coryli Le Quesne 1977 and Edwardsiana staminata (Ribaut, 1931) were recognized for the first time. Clearly parasitized and apparently unparasitized leafhoppers and dissected dryinid larvae were assayed by polyacrylamide gel electrophoresis. The α-glycerophosphate dehydrogenase (α-GPD) enzyme system proved to be a reliable tool for indicating the presence of dryinids in all sampled species: the parasitized adults always showed a fast band, which was absent in unparasitized adults. The α-GPD was a reliable enzyme system to detect dryinids at an early stage of their development but not to discriminate among dryinid species. The occurrence of dryinids in the males of A. coryli and Zygina rhamni Ferrari, 1882 was also pointed out by the change of their colouration.

scholarly journals Allozyme pattern for new record of Craspedacusta sowerbii in Serbia

2004 ◽  
pp. 15-19 ◽  
Author(s):  
Jasmina Ludoski ◽  
Vesna Milankov ◽  
Predrag Radisic
Keyword(s):  
Genetic Variability ◽  
Natural Population ◽  
Gel Electrophoresis ◽  
New Record ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Serbia And Montenegro ◽  
Enzyme Loci ◽  
First Time

Cosmopolitan freshwater jellyfish Craspedacusta sowerbii L a n k e s t e r 1880 (Cnidaria, Hydrozoa) was recorded for the first time in the lake Velika peskara near Zrenjanin (Serbia and Montenegro) in summer 1998. A natural population of C. sowerbii from the lake Velika peskara was analyzed for genetic variability at 9 enzyme loci (Gpi, Hk, Idh-1, Idh-2, Me, Mdh-1 Mdh-2, Pgm and Sod) by polyacrylamide gel electrophoresis. A zymogram indicated that population was monomorphic at all analyzed loci.

Isolation of size homogeneous preparations of high molecular weight and low molecular weight fibrinogens

1981 ◽  
Vol 59 (5) ◽  
pp. 332-342 ◽  
Author(s):  
Hannah M. Phillips
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Molecular Sizes ◽  
Carboxyl Terminal ◽  
First Time ◽  
Molecular Weight Form

Molecular sizes of fibrinogen (F) similar to FI, higher molecular weight form, and FII, lower molecular weight form, have been found by Lipinska and colleagues. A procedure has been developed to isolate for the first time each of the FI and FII forms of fibrinogen which are free of each other and of high molecular weight fibrin–fibrinogen complexes. This process involved removing the complexes by A-5 m chromatography. This chromatography also reduced a protein contaminant (X) and removed plasminogen. (NH4)2SO4 subfractionation at pH 5.9 was then done. A subtraction (16–18%) containing 90% FI and another (22–25% or 25–28%) containing 96% FII were obtained. Reprecipitation of the first 16–18% subfraction yielded a subfraction containing 97% FI. Sodium dodecyl sulfate (SDS) – polyacrylamide gel electrophoresis of FII revealed that it contains one intact Aα chain per (Bβ, γ)2. Clot opacity studies on FII suggested that the carboxyl terminal portion of the α chain of fibrin plays an important role in the lateral associations in fibrin polymerization.Also, the pattern of (NH4)2SO4 precipitation of the endogenous fibrin–fibrinogen complexes was studied. This revealed that the complexes precipitated mostly in the least soluble subfractions, but small amounts could be found in all subfractions. Examination of the complexes by SDS–polyacrylamide gel electrophoresis showed that most of the complexes could be dissociated to FI and FII. However, there were complexes which remained and these were found to be covalently cross-linked forms probably produced by factor XIII.

Ultrastructural localization of specific nucleoprotein fractions

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).

Platelet Microtubule Subunit Proteins

1979 ◽  
Vol 42 (05) ◽  
pp. 1630-1633 ◽  
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.

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

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.

Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

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.

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

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

<em>Bahan<strong> </strong>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).<strong> </strong>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.</em>

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