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.

Cyst Membrane Protein Composition as a Discriminant Character in the Genus Artemia. (International Study on Artemia LV)

1997 ◽  
Vol 77 (1) ◽  
pp. 265-268 ◽  
Author(s):  
T.J. Abatzopoulos ◽  
G.V. Triantaphyllidis ◽  
J.A. Beardmore ◽  
P. Sorgeloos
Keyword(s):  
Membrane Protein ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Protein Composition ◽  
International Study ◽  
Fibrous Layer ◽  
Cuticular Membrane ◽  
Cyst Membrane

Isolated embryonic membranes (i.e. the outer cuticular membrane, the fibrous layer, the inner cuticular membrane and the hatching membrane) and homogenates of incubated, decapsulated cysts of 16 populations from five Artemia species (Crustacea, Anostraca) were examined by sodium dodecyl-sulphate polyacrylamide gel electrophoresis. Characteristic differences in major polypeptides between 45 and 205 kD were seen. These differences might be used as markers for identification of different Artemia species. The validity of this approach in characterizing Artemia populations is discussed.

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.

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 the protein responsible for pyruvate transport into rat liver and heart mitochondria by specific labelling with [3H]N-phenylmaleimide

1981 ◽  
Vol 196 (2) ◽  
pp. 471-479 ◽  
Author(s):  
A P Thomas ◽  
A P Halestrap
Keyword(s):  
Membrane Protein ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Mitochondrial Protein ◽  
Sodium Dodecyl ◽  
Liver Mitochondria ◽  
Heart Mitochondria ◽  
Approximate Amount ◽  
Specific Labelling

1. N-Phenylmaleimide irreversibly inhibits pyruvate transport into rat heart and liver mitochondria to a much greater extent than does N-ethylmaleimide, iodoacetate or bromopyruvate. alpha-Cyanocinnamate protects the pyruvate transporter from attack by this thiol-blocking reagent. 2. In both heart and liver mitochondria alpha-cyanocinnamate diminishes labelling by [3H]N-phenylmaleimide of a membrane protein of subunit mol.wt. 15000 on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 3. Exposure of mitochondrial to unlabelled N-phenylmaleimide in the presence of alpha-cyanocinnamate, followed by removal of alpha-cyanocinnamate and exposure to [3H]N-phenylmaleimide, produced specific labelling of the same protein. 4. Both labelling and kinetic experiments with inhibitors gave values for the approximate amount of carrier present in liver and heart mitochondria of 100 and 450 pmol/mg of mitochondrial protein respectively. 5. The turnover numbers for net pyruvate transport and pyruvate exchange at 0 degrees C were 6 and 200 min-1 respectively.

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 Calcium-dependence of insulin receptor phosphorylation

1983 ◽  
Vol 214 (2) ◽  
pp. 361-366 ◽  
Author(s):  
W E Plehwe ◽  
P F Williams ◽  
I D Caterson ◽  
L C Harrison ◽  
J R Turtle
Keyword(s):  
Membrane Protein ◽  
Insulin Receptor ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Beta Subunit ◽  
Receptor Phosphorylation ◽  
32P Incorporation ◽  
Isolated Rat

Phosphorylation of the insulin receptor of isolated rat adipocytes in response to insulin has been studied. Immunoprecipitation of adipocyte membrane protein demonstrated increased incorporation of 32P after exposure to insulin for 15 min, but this was dependent on the presence of physiological concentrations of Ca2+ and Mg2+. Autoradiography of solubilized immunoprecipitated membrane protein after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis revealed that most of the 32P incorporation occurred in a band corresponding to Mr 95 000, which has been identified previously as the beta-subunit of the insulin receptor. 32P incorporation was inhibited by 2,4-dinitrophenol and trifluoperazine. It is suggested that insulin-receptor phosphorylation is an energy-requiring process that is Ca2+-dependent and may be modulated by calmodulin. Phosphorylation may proceed independently of glucose transport.

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