scholarly journals Electrophoretic Protein Banding Patterns among Penicillium Strains Isolated from Saudi Arabia

2014 ◽  
Vol 2 (3) ◽  
pp. 283-290 ◽  
Author(s):  
Ehab Abdel-Razik Kamel ◽  
M. Elsayed Rashed

14 strains of Penicillium species were isolated from different localities and habitats from Jeddah, Saudi Arabia and cultivated on two different media: Czapek Dox’s medium, in which NaNO3 is the source of inorganic nitrogen, and Waksman’s medium, in which pepton is the source of organic nitrogen. Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE) technique was used in this study to distinguish these isolates. The Penicillium isolates examined in this study consisted of six Penicillium species: Penicillium corylophilum (three isolates), P. rubrum (one isolate), P. citrinum (two isolates), P. crustosum (one isolate), P. canesens (six isolates) and Penicillium sp. (one isolate). The electrophoretic protein patterns from Penicillium isolates grown on Czapek Dox's medium revealed the presence of 17 different bands (out of 14 polymorphic bands, there were three monomorphic bands and two unique bands). The electrophoretic protein pattern of the same isolates grown on Waksman's medium revealed the presence of 12 different bands (out of eight polymorphic bands, there were four monomorphic bands and one unique band). Data were analysed by a clustering method and similarity coefficients using NTSYSpc version 2.02i. Two different phenograms were produced for the studied Penicillium species based on the analysis of the protein banding patterns. Data from the protein banding patterns produced from both media were combined and analysed to produce third phenogram, and the relationships between the species and isolates are discussed. DOI: http://dx.doi.org/10.3126/ijasbt.v2i3.10949Int J Appl Sci Biotechnol, Vol. 2(3): 283-290  

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.


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.


1996 ◽  
Vol 51 (5-6) ◽  
pp. 342-354 ◽  
Author(s):  
Beate Nicolaus ◽  
Yukiharu Sato ◽  
Ko Wakabayashi ◽  
Peter Böger

Abstract Thiadiazolidine-converting activity (isomerase), detected in a 45-75% ammonium sulfate precipitate from corn seedlings extracts, was purified by chromatography on hydroxyapatite and by anion exchange on Mono Q Sepharose. Two fractions 1 and 2 with isomerase activity were separated on Mono Q by combination of a stepwise elution and continuous salt gradient; fraction 2 eluting at higher salt concentrations was found the most active. Total activity could be enhanced by treatment of seedlings with naphthalic anhydride. Both fractions containing isomerase activity were further purified by glutathione-(GSH) agarose affinity chromatography and characterized by their specificity for different thiadiazolidines. Sodium dodecyl sulfate polyacrylamide gel electrophoresis and gel filtration revealed that the isomerase of fraction 2 consists either of a homodimer or a heterodimer of two proteins with apparent molecular weights of 28 and 31 kDa, respectively. The protein pattern as well as the strict dependence of activity on thiol groups (GSH or dithiothreitol) suggested a glutathione Stransferase (GST) catalyzing the thiadiazolidine conversion. Further evidence was obtained by measuring reactions specific for GSTs in both purified fractions, namely the conjugating activity for l-chloro-2,4-dinitrobenzene (CDNB ). atrazine and metazachlor. While no atrazine turnover was found, metazachlor and CDNB conjugation occurred rapidly. Both fractions differed in their activities to several GST substrates with fraction 2 being more effective in metazachlor but less active in C DN B conjugation. Inhibitors specific for GST-catalyzed reactions also inhibited thiadiazolidine conversion confirming that isomerizing activity is attributed to a GST form. We conclude that GST isoforms with different affinities towards thiadiazolidines have been isolated. CDNB activity, molecular weight, the protein pattern on SDS-PAGE as well as the amino acid sequence of one of its polypeptides suggest that fraction 1, less active in thiadiazolidine isomerization, is identical to GST I. The second peptide of this fraction was resistant to Edman degradation probably due to N-terminal blockage. The properties of the high isomerase activity found in fraction 2 are in agreement with characteristics of a GST previously termed as isoform II.


2000 ◽  
Vol 68 (3) ◽  
pp. 1048-1053 ◽  
Author(s):  
Cuong Vuong ◽  
Friedrich Götz ◽  
Michael Otto

ABSTRACT The physiological significance of the accessory gene regulator (agr) system of Staphylococcus epidermidis was investigated by construction of an agr deletion mutant via allelic replacement with a spectinomycin resistance cassette. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis showed that the protein pattern was strongly altered in the mutant; the amounts of most surface proteins were higher, whereas the amounts of most exoproteins were lower. The agrsystem of S. epidermidis thus appears to have an important impact on growth phase-dependent protein synthesis as has been shown for Staphylococcus aureus. The activity of the exoenzymes lipase and protease, assumed to be involved in staphylococcal pathogenicity, was investigated by agar diffusion assays and SDS-PAGE activity staining. A general reduction of these enzyme activities in the agr mutant was found. The difference in overall lipase activity was small, but zymographic analysis suggested a clear defect in lipase processing in the agr mutant.


1995 ◽  
Vol 75 (1) ◽  
pp. 191-193
Author(s):  
S. J. Molnar ◽  
A. McKay

Restriction fragment length polymorphisms (RFLP) at the hordein loci were compared with hordein protein patterns for discrimination of barley cultivars. RFLP banding patterns documented extensive polymorphism for B and C hordein gene families in eight closely related western Canadian two-rowed barley cultivars, five parental cultivars and a U.K. cultivar. RFLP results were compared with published protein pattern data on the same cultivars. The power to discriminate cultivars by the two methods is similar. Key words: RFLP, hordein, barley, Hordeum vulgare, cultivar identification


2008 ◽  
Vol 71 (11) ◽  
pp. 2289-2294 ◽  
Author(s):  
MING-LUN CHIANG ◽  
WEI-LI HO ◽  
ROCH-CHUI YU ◽  
CHENG-CHUN CHOU

Cells of Vibrio parahaemolyticus 690 were subjected either to heat shock at 42°C for 45 min or to ethanol shock in the presence of 5% ethanol for 60 min. The protein profiles of the unstressed and stressed V. parahaemolyticus cells were compared. Additionally, the induction of DnaK- and GroEL-like proteins in the unstressed and stressed cells of V. parahaemolyticus was also examined. Analysis with one-dimensional sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) indicated that three proteins with molecular masses of 93, 77, and 58 kDa were induced by both heat shock and ethanol shock. The protein patterns revealed by two-dimensional electrophoresis were more detailed than those revealed by one-dimensional SDS-PAGE. It was found that heat shock and ethanol shock affected the expression of a total of 28 proteins. Among them, four proteins with molecular masses of 94, 32.1, 26.7, and 25.7 kDa were enhanced by both heat shock and ethanol shock. Furthermore, immunoblot analysis showed the presence of a GroEL-like protein with a molecular mass of 61 kDa in the test organism, with the heat-shocked and ethanol-shocked cells producing a GroEL-like protein in a larger quantity than the unstressed cells. However, DnaK-like protein was not detectable in either the unstressed or the stressed cells.


1992 ◽  
Vol 4 (2) ◽  
pp. 249 ◽  
Author(s):  
A Paliwal ◽  
B Malaviya ◽  
VP Kamboj

Oviducts were obtained from monkeys on Days 8, 14, 19 and 25 of the menstrual cycle and changes in the pattern of luminal fluid proteins were examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Densitometric analysis after periodic acid Schiff's reagent (PAS) and coomassie blue staining of the gels revealed 85 and 95 kDa proteins only up to Day 14 whereas a 130 kDa glycoprotein persisted up to Day 19 and reached a nadir at mid-menstrual cycle (Day 14). The absence of the 130 kDa glycoprotein in the serum and its presence in cytosolic preparations up to Day 19 suggest that it is of oviductal origin. The 130 kDa glycoprotein is of particular interest since it was present in the oviductal fluid during mid cycle, a period when the oviduct participates in gamete transport, fertilization and embryo development. The conclusion drawn from this study is that the protein profile of monkey oviductal fluid changes during the menstrual cycle.


1989 ◽  
Vol 1 (2) ◽  
pp. 165-169 ◽  
Author(s):  
Shaohua Zhao ◽  
Richard Yamamoto

Strains of Mycoplasma iowae were homogeneous in some characteristics and heterogeneous in others. Thus, the biochemical tests, immunofluorescence, and protein profiling by sodium dodecyl sulfate-polyacrylamide gel electrophoresis were group-specific tests. However, some minor differences in protein patterns were seen among strains. The growth inhibition test tended to be strain-specific. Hemagglutination titers were very low and unstable for the majority of strains. One strain (RY-65) with a stable high-titer hemagglutinin failed to react in the hemagglutination-inhibition test against immune sera to the reference strains. Restriction endonuclease DNA analyses was the most useful method to differentiate 1 strain from another.


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