scholarly journals Albumin obscures sex differences in blood protein patterns of rats and humans

1980 ◽  
Vol 191 (3) ◽  
pp. 869-872 ◽  
Author(s):  
D M Gersten ◽  
B S Khirabadi ◽  
P Kurian ◽  
R S Ledley ◽  
T Mahany ◽  
...  
Keyword(s):  
Gel Electrophoresis ◽  
Protein Pattern ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Female Rats ◽  
Blood Protein ◽  
Protein Patterns ◽  
Male And Female ◽  
Reducing Conditions ◽  
Male And Female Rats

Sex related differences in the blood protein patterns of male and female rats and humans have been studied by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. In rats, a prominent band of mol.wt. 74000–78000 is seen in females in far greater quantity than in males, castrated males or ovariectomized females. A secondary band of 100000 is seen under non-reducing conditions in female rats that is absent in males. In humans, bands of 92000 and 88000 mol.wt. appear to be variable in concentration in men although relatively constant in women. The above differences are observable only if serum albumin is removed from the samples before electrophoresis. The results suggest that each sex has its own characteristic blood protein pattern.

scholarly journals Identification of outbreak-associated and other strains ofClostridium difficileby numerical analysis of SDS-PAGE protein patterns

1994 ◽  
Vol 113 (1) ◽  
pp. 1-12 ◽  
Author(s):  
M. Costas ◽  
B. Holmes ◽  
M. Ganner ◽  
S. L. W. On ◽  
P. N. Hoffman ◽  
...  
Keyword(s):  
Numerical Analysis ◽  
High Resolution ◽  
Clostridium Difficile ◽  
Gel Electrophoresis ◽  
Protein Pattern ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Patterns ◽  
One Dimensional ◽  
Sds Page

SUMMARYSeventy-three cultures ofClostridium difficileisolated both during, and in the period immediately following, an outbreak of infection in a group of three hospitals, were characterized by one-dimensional sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS–PAGE) of whole-cell proteins. Each protein pattern was characterized by the presence of one or two dense bands which were highly reproducible. The protein patterns were used as the basis for a numerical analysis which divided the strains into five phenons (electrophoretic or EP types). The majority, 60 of the 73 cultures, belonged to a single phenon which included strains from both patients and the environment. We conclude that high-resolution SDS–PAGE of proteins provides an effective method for typingC. difficileand therefore for tracing the possible spread of epidemic strains in hospitals and other institutions, thereby allowing a better understanding of the epidemiology of the organism.

Interpopulation study of three Artemia strains from South India based on cyst membrane proteins

2006 ◽  
Vol 86 (5) ◽  
pp. 1097-1100
Author(s):  
V. Sugumar ◽  
N. Munuswamy
Keyword(s):  
Membrane Protein ◽  
Gel Electrophoresis ◽  
South India ◽  
Protein Pattern ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Fibrous Layer ◽  
Protein Patterns ◽  
Cuticular Membrane ◽  
Cyst Membrane

Isolated embryonic membranes (i.e. the outer cuticular membrane, the fibrous layer, the inner cuticular membrane and the hatching membrane) of a bisexual and two parthenogenetic strains from South India were examined using sodium dodecyl-sulphate polyacrylamide gel electrophoresis. Interpopulation comparison of the protein patterns revealed variations in the major polypeptides between the three populations. Repeated analyses of the embryonic membrane protein pattern of the same population resulted in the same banding pattern suggesting that the method is reproducible. These differences might be used as markers for identification of different Artemia strains.

Variation in goat fibre protein

1989 ◽  
Vol 40 (3) ◽  
pp. 675 ◽  
Author(s):  
DJ Tucker ◽  
AHF Hudson ◽  
A Laudani ◽  
RC Marshall ◽  
DE Rivett
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Apparent Molecular Weight ◽  
Wool Fibre ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Cashmere Goats

The proteins from a range of cashmere, mohair, angoratcashmere crossbred and wool fibre samples were extracted at pH 8 with 8 M urea containing dithiothreitol, and were then radiolabelled by S-carboxymethylation using iodo(2-14C) acetate. The proteins from each sample were examined by two dimensional polyacrylamide gel electrophoresis in which the separation in the first dimension was according to charge at pH 8.9 and in the second dimension according to apparent molecular weight in the presence of sodium dodecyl sulfate. After electrophoresis the proteins were detected by fluorography. Protein differences in keratin samples from some individual goats existed, although the overall protein patterns were similar. None of the differences were consistent with any one goat fibre type. The protein patterns obtained for fibre samples from individual cashmere goats showed some differences when compared to those found for commercial blends from the same country of origin, indicating that blending can mask any animal-to-animal variation. While the electrophoretic technique does not unequivocally distinguish between cashmere, mohair and angora/cashmere crossbred fibres it does differentiate between wool and goat fibres.

scholarly journals Albumin associated with purified pig lymphocyte plasma membrane

1980 ◽  
Vol 192 (1) ◽  
pp. 49-57 ◽  
Author(s):  
M J Owen ◽  
B H Barber ◽  
R A Faulkes ◽  
M J Crumpton
Keyword(s):  
Plasma Membrane ◽  
Serum Albumin ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Membrane Fraction ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Reducing Conditions ◽  
Isoelectric Points ◽  
Pig Serum

Plasma-membrane preparations purified from pig lymphocytes contained a major polypeptide component of mol.wt. about 68 000. This component was identified as pig albumin by the following comparisons with authentic pig serum albumin: (a) co-migration when analysed by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis under reducing and non-reducing conditions; (b) identical isoelectric points; (c) similar “fingerprints” of arginine-containing tryptic peptides; (d) reactivity with anti-(pig albumin) serum. The albumin was bound tightly to the plasma membrane. Biosynthetic labelling of pig lymphocytes under a variety of conditions failed to provide evidence that albumin was synthesized by lymphocytes, suggesting that the plasma-membrane-associated albumin was of extraneous origin. Radiolabelled pig serum albumin, however, failed to bind to the plasma-membrane fraction when added before cell disruption. Although lymphocyte plasma membrane preparations from other species possessed a polypeptide of about 68 000 mol.wt., this was judged not to be albumin on the basis of electrophoretic mobility under non-reducing conditions; also, no polypeptide was precipitated by anti-albumin sera. It is concluded that pig lymphocyte plasma-membrane preparations possess albumin which, although firmly attached, was probably of extraneous origin. This association appeared not to be common to lymphocytes from other species.

STUDIES OF A THYROID HORMONE AND ANDROGEN DEPENDENT PROTEIN IN RAT LIVER CYTOSOL

1977 ◽  
Vol 84 (3) ◽  
pp. 548-558 ◽  
Author(s):  
Wolfgang H. Dillmann ◽  
Enrique Silva ◽  
Martin I. Surks ◽  
Jack H. Oppenheimer
Keyword(s):  
Molecular Weight ◽  
Thyroid Hormone ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Female Rats ◽  
Male Rats ◽  
Male Rat ◽  
Liver Cytosol

ABSTRACT Sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis of the liver cytosol of euthyroid male rats revealed a prominent band (molecular weight, 26 000 daltons), designated Protein II, which was virtually absent in the cytosol of hypothyroid animals. Injection of 500 μg triiodothyronine (T3) per 100 g body weight resulted in a maximal increase in the level of Protein II, reaching 90% of the euthyroidal level 3 days after hormone administration. Concomitant studies with the liver mitochondrial enzyme alpha-glycerophosphate dehydrogenase (α-GPD) indicated that this T3 dose also resulted in a maximal enzyme response in this time period. Since we have estimated that 500 μg of T3 will saturate nearly all nuclear T3 binding sites, these results support the concept that the synthesis of both proteins is limited by nuclear binding. Protein II was absent in the liver cytosol of female rats but could be induced in ovariectomized female rats by androgens. Treatment of male rats with oestradiol resulted in disappearance of Protein II. Since administration of testosterone to hypothyroid male rats caused only a minimal increase in the amount of Protein II, the absence of the protein in hypothyroid animals was not due to androgen deficiency. Similarities in the molecular weight and the response to hormonal manipulation of Protein II and of the urinary α2uglobulin, previously reported by Roy (1973) raise the possibility that these proteins are the same. The high concentration of Protein II in male rat cytosol and the relative ease in its identification by SDS polyacrylamide gel electrophoresis make it a potentially useful model protein for the study of thyroid hormone action at the cellular level.

scholarly journals Purification and characterization of a plasminogen activator secreted by a pig kidney cell line

1984 ◽  
Vol 219 (3) ◽  
pp. 971-978 ◽  
Author(s):  
M Sudol ◽  
E Reich
Keyword(s):  
Plasminogen Activator ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Pig Kidney ◽  
Reducing Conditions ◽  
Pig Kidney Cells

The plasminogen activator secreted by calcitonin-treated pig kidney cells was purified, characterized and compared with human urinary urokinase. The purification procedure was based on the following steps: sulphopropyl-Sephadex chromatography, p-aminobenzamidine-Sepharose chromatography, preparative sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and isoelectrofocusing. The purified enzyme was obtained from the conditioned medium with a yield of 13% and a purification factor of 390-fold. Analysis by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis under non-reducing conditions showed one closely spaced doublet with an Mr of 50 000; in the presence of reducing agents, two additional bands of Mr 30 000 and 20 000 appeared. The purified enzyme resembles the 53 000-Mr components of human urinary urokinase in amino acid composition and two-dimensional tryptic peptide maps and in its catalytic properties, and the two enzymes cross-react immunologically with rabbit antibodies raised against either. The enzyme appears to be different from tissue plasminogen activator secreted by HeLa cells.

scholarly journals Repression, Derepression and Activation of Nitrogenase in Azotobacter Vinelandii

1976 ◽  
Vol 29 (2) ◽  
pp. 147 ◽  
Author(s):  
DJD Nicholas ◽  
Judy V Deering
Keyword(s):  
Gel Electrophoresis ◽  
Azotobacter Vinelandii ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Ferrous Ammonium Sulphate ◽  
Ammonium Ions ◽  
Protein Patterns ◽  
S Protein ◽  
Immunological Tests ◽  
Ferrous Ammonium

Ammonium ions repressed nitrogenase in cells fixing N2 gas. Immunological tests and electrophoresIs in various gels show that component I (Fe-Mo-S protein) was completely repressed by ammonium, whereas component II (Fe-S protein) apoprotein was not markedly affected. Component II from ammonium-grown cells, however, was inactive since it did not cross react with component I to reduce C2H2 to C2H4 ? The inactive component II apoprotein is immunologically identical to its active counterpart from cells fixing N2 ? Identical protein patterns were also observed in various gel-electrophoresis systems. Oxygen-inactivated component II may be reactivated with FeS04' This salt is preferable to ferrous ammonium sulphate which inactivated component I. Immunodiffusion under aerobic conditions shows that purified component I is composed of aggregated and non-aggregated forms which are antigenically distinct. The aggregate was dissociated by treatment with sodium dodecyl sulphate (SDS) into a single antigenic species which was further resolved into two subunits on SDS disc polyacrylamide gel electrophoresis.

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