Serum protein fractions from children of differing nutritional status analysed by polyacrylamide gel electrophoresis and electroimmunoassay

1. The nutritional status of children showing no clinical signs of malnutrition, from the University School of Khon Kaen, Khon Kaen province, north-east Thailand and from two villages nearby, was tested. The children were grouped according to their body-weight expressed as a percentage of expected weight-for-height (Harvard standards (Stuart & Stevenson, 1959), as given by Jelliffe (1966))..2. The differing prealbumin concentrations indicated that nutritional status differed between the groups..3. The urinary urea: creatinine ratio was significantly lower in the village children compared with the children from Khon Kaen, indicative of the higher dietary protein intake of the latter..4. α1-Acid glycoprotein and the first ‘post-albumin peak’ (obtained by polyacrylamide gel electrophoresis of serum and containing mainly Gc-globulin, α1-antichymotrypsin and α1-B-glycoprotein) were found to be significantly higher in the village children compared with children from Khon Kaen..5. The three main proteins of the first ‘post-albumin peak’ from polyacrylamide gel electrophoresis of serum were tested separately using the electroimmunoassay method. There was no significant difference in Gc-globulin between the children from Khon Kaen and the village children. The concentration of α1-B-glycoprotein from those Khon Kaen children whose body-weight was more than 95% expected weight-for-height was significantly lower compared with that of village children. α1-Antichymotrypsin concentration was significantly higher in serum from Khon Kaen children than in serum from village children.

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Effects of triiodothyronine and nutritional status on nuclear non-histone proteins of the rat liver

Acta Endocrinologica ◽

10.1530/acta.0.1020567 ◽

1983 ◽

Vol 102 (4) ◽

pp. 567-571 ◽

Cited By ~ 1

Author(s):

Cristiana E. Juge-Aubry ◽

Kurt Bachmann ◽

Albert G. Burger

Keyword(s):

Single Dose ◽

Nutritional Status ◽

Thyroid Hormones ◽

Present Article ◽

Rat Liver ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Polyacrylamide Gel ◽

Rapid Response ◽

Intact Rats

Abstract. In the hepatic nucleus of the rat at least 2 nuclear globulin bands, identified by SDS polyacrylamide gel electrophoresis, are known to be influenced by thyroid hormones. In the present article a quantitation of these bands was obtained by scanning techniques. The effects of T3 were studied in male thyroidectomized (Tx) and intact rats. After sacrifice the hepatic nuclear globulins were prepared according to published methods. In Tx rats substituted with a single dose of 50 μg or during one week 2 μg T3 the t band decreased from 5.3% to 2.7% of the total nuclear globulin content which represent a complete normalisation. The n band did not show this rapid response to T3 as 2 μg given for one week only partially restored this band (Tx 1.4%,Tx + T32.2%). However during starvation of intact rats only the n band was slightly influenced by T3 as 2 μg of T3 partially prevented the decrease of this band seen in untreated euthyroid starving rats. The increase of the t band in starvation was not affected by T3. In conclusion: the n and t bands are controlled by several factors, two of which are T3 and nutrition. The control of the t band seems to be dominated by the nutritional status of the animal. T3 seems to keep some activity on the n band, even in starved rats.

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Molecular epidemiology of human rotavirus

Journal of Hygiene ◽

10.1017/s0022172400066043 ◽

1986 ◽

Vol 96 (2) ◽

pp. 265-275 ◽

Cited By ~ 5

Author(s):

P. Cash ◽

E. Freebain ◽

T. Brown ◽

T. M. S. Reid

Keyword(s):

Molecular Epidemiology ◽

Gel Electrophoresis ◽

Polyacrylamide Gel Electrophoresis ◽

Hospitalized Patients ◽

Polyacrylamide Gel ◽

Age Group ◽

Peak Incidence ◽

North East ◽

Human Rotavirus ◽

Epidemic Period

SUMMARYThe epidemiology of human rotavirus (HRV) in north-east Scotland was investigated between 1982 and 1984. During this period 708 HRV infections were recorded. The majority (83%) of the infections were in children less than 5 years of age although some were recorded in adults. The peak incidence occurred in the winter months although a high number of HRV infections was reported during the summer of 1983. A total of 840 faecal specimens containing rotavirus were screened for HRV genome RNA by polyacrylamide gel electrophoresis. Seven hundred (83%) specimens gave RNA profiles suitable for establishing the HRV electrophoretype. Twenty-five different electrophoretypes were identified, of which 21 had ‘long’ RNA profiles and four had ‘short’ RNA profiles. There was extensive co-circulation of distinct electrophoretypes although during any one epidemic period the majority of viruses belonged to a relatively small number of types. Comparison of viruses collected from hospitalized and non-hospitalized Patients showed no differences in electrophoretype distribution. HRV was identified in faecal specimens from a wide age group and no correlation was demonstrated between age of patient and electrophoretype of the infecting virus.

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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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