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

1976 ◽  
Vol 29 (2) ◽  
pp. 147 ◽  
Author(s):  
DJD Nicholas ◽  
Judy V Deering

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.

1989 ◽  
Vol 40 (3) ◽  
pp. 675 ◽  
Author(s):  
DJ Tucker ◽  
AHF Hudson ◽  
A Laudani ◽  
RC Marshall ◽  
DE Rivett

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.


1994 ◽  
Vol 113 (1) ◽  
pp. 1-12 ◽  
Author(s):  
M. Costas ◽  
B. Holmes ◽  
M. Ganner ◽  
S. L. W. On ◽  
P. N. Hoffman ◽  
...  

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.


2006 ◽  
Vol 86 (5) ◽  
pp. 1097-1100
Author(s):  
V. Sugumar ◽  
N. Munuswamy

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.


1980 ◽  
Vol 191 (3) ◽  
pp. 869-872 ◽  
Author(s):  
D M Gersten ◽  
B S Khirabadi ◽  
P Kurian ◽  
R S Ledley ◽  
T Mahany ◽  
...  

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.


1983 ◽  
Vol 61 (11) ◽  
pp. 2919-2923 ◽  
Author(s):  
David R. Benson ◽  
Deborah Hanna

Procedures for estimating the diversity of Frankia isolates are described. Forty-three alder isolates were separated into six groups by comparing protein patterns obtained during sodium dodecyl sulfate – polyacrylamide gel electrophoresis (SDS–PAGE) of whole-cell lysates. Thirty-five of the strains comprised group A and were indistinguishable from one another. Four strains were quite similar to a Comptonia peregrina isolate (CpI1) and were included in group C. Group D had two members and groups B, E, and F each had one member. The groupings were confirmed by hyphal morphology, colony appearance, and carbon source utilization patterns.


1996 ◽  
Vol 79 (6) ◽  
pp. 1466-1470 ◽  
Author(s):  
Emiko Mochizuki ◽  
Takao Yamamoto ◽  
Sumiko Suzuki ◽  
Hiroyuki Nakazawa

Abstract We developed a rapid and simple method for identifying garlic and garlic products using sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) with silver staining. Samples were homogenized with 1 % SDS or 6M urea and centrifuged. Supernatant containing garlic proteins was mixed with the same volume of loading buffer containing SDS and mercaptoethanol, heated in boiling water for 2 min, and applied to the wells of a ready-to-use polyacrylamide gradient gel (4–20%). Electrophoresis was performed 20 mA constant current for 2 h. The gel was stained with a silver staining kit and dried. Protein patterns of garlic and garlic products are different from those of other Allium plants such as onion, rakkyo, and caucas. The method was used to analyze samples of spice and garlic clove products. Absence of protein bands in garlic extract products suggests the products may contain less proteins and/or denatured proteins.


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