Effects of polybrominated biphenyls upon rat urinary protein patterns as detected by two-dimensional electrophoresis

1987 ◽  
Vol 16 (5) ◽  
pp. 579-585
Author(s):  
James E. Myrick ◽  
Mary K. Robinson ◽  
Ivey Lois Hubert ◽  
S. Jay Smith ◽  
W. Harry Hannon
Keyword(s):  
Urinary Protein ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Two Dimensional Electrophoresis ◽  
Polybrominated Biphenyls ◽  
Dimensional Electrophoresis

Plasma apolipoprotein pattern in fish-eye disease examined by high-resolution two-dimensional electrophoresis.

1985 ◽  
Vol 31 (12) ◽  
pp. 2032-2035 ◽  
Author(s):  
T Marshall ◽  
K M Williams ◽  
L Holmquist ◽  
L A Carlson ◽  
O Vesterberg
Keyword(s):  
High Resolution ◽  
Plasma Proteins ◽  
Eye Disease ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Two Dimensional Electrophoresis ◽  
Significant Difference ◽  
Fish Eye ◽  
Dimensional Electrophoresis ◽  
Plasma Apolipoprotein

Abstract We compared the plasma protein patterns of the two living patients suffering from fish-eye disease with those of appropriate controls, using high-resolution two-dimensional electrophoresis. Quantitative abnormalities were detected in plasma polypeptides corresponding to the isoforms of apolipoproteins A-I and A-II. The disease was characterized by normal concentrations of proapo A-I but dramatically subnormal concentrations of the other apo A-I isoforms and apo A-II. No significant difference was detected in the concentrations of other plasma proteins. These findings are discussed in relation to other apolipoprotein disorders.

scholarly journals Evaluation of six different protocols for protein extraction from rice young panicles by two-dimensional electrophoresis

2020 ◽  
Author(s):  
Xiaoping Huang ◽  
Hui-wen Zhou
Keyword(s):  
Protein Concentration ◽  
Protein Extraction ◽  
Image Resolution ◽  
Plant Tissues ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Molecular Weight Range ◽  
Two Dimensional Electrophoresis ◽  
Phenol Extraction ◽  
Dimensional Electrophoresis

Abstract Background: For most reported proteomics approaches, protein extraction are of crucial importance for optimal results. However, extraction of protein from plant tissues still exist great challenges due to low protein content and many secondary metabolites that prominently interfering with isoelectric focusing. Up to now, no attempts are focused on comparison of protein extraction from rice young panicles.Methods: To establish a higher efficiency protein extraction protocol suited for two-dimensional electrophoresis in rice young panicles, six protocols for protein preparation were evaluated in terms of protein concentration, the molecular weight range of protein, gel image resolution, the number of protein spots: 1) Phenol extraction; 2) Mg/Nonidet P-40 (NP-40) extraction; 3) Tris-Base/acetone extraction; 4) SDS extraction; 5) trichloroacetic acid (TCA)/acetone/phenol extraction; 6) TCA/acetone precipitation.Results: The result explicitly demonstrated that TCA/acetone/phenol method provided a high-enhanced protein extraction efficacy from rice young panicles than other protocols in terms of the protein concentration (9.79±0.23 SD), the most comprehensive proteins (10 KDa to 150 KDa), the maximum number of protein spots (450±53 SD), the greater gel image resolution and spot abundance. In addition, these methods also generated remarkably differential 2-DE protein patterns. Twenty-nine of 30 visible differentially extracted proteins were identified by MS analysis and were divided into eight categories. Prediction for protein subcellular localization and grand average of hydropathy (GRAVY) analysis showed that certain special proteins respectively necessitate different extraction methods due to different physicochemical properties of each protocol.Conclusions: Overall, this paper will facilitate to provide a cornerstone of comparative proteomic analysis from rice young panicles, including other complicated plant tissues.

scholarly journals Two-Dimensional Electrophoresis Study of Lactobacillus delbrueckii subsp. bulgaricus Thermotolerance

2002 ◽  
Vol 68 (3) ◽  
pp. 1055-1063 ◽  
Author(s):  
Gwenola Gouesbet ◽  
Gwenael Jan ◽  
Patrick Boyaval
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Lactobacillus Delbrueckii ◽  
Original Strain ◽  
Two Dimensional ◽  
Cell Recovery ◽  
Protein Patterns ◽  
Heat Stress Response ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

ABSTRACT The response of Lactobacillus delbrueckii subsp. bulgaricus cells to heat stress was studied by use of a chemically defined medium. Two-dimensional electrophoresis (2-DE) analysis was used to correlate the kinetics of heat shock protein (HSP) induction with cell recovery from heat injury. We demonstrated that enhanced viability, observed after 10 min at 65°C, resulted from the overexpression of HSP and from mechanisms not linked to protein synthesis. In order to analyze the thermoadaptation mechanisms involved, thermoresistant variants were selected. These variants showed enhanced constitutive tolerance toward heat shock. However, contrary to the wild-type strain, these variants were poorly protected after osmotic or heat pretreatments. This result suggests that above a certain threshold, cells reach a maximum level of protection that cannot be easily exceeded. A comparison of protein patterns showed that the variants were able to induce more rapidly their adaptive mechanisms than the original strain. In particular, the variants were able to express constitutively more HSP, leading to the higher level of thermoprotection observed. This is the first report of the study by 2-DE of the heat stress response in L. delbrueckii subsp. bulgaricus.

scholarly journals Use of Two-Dimensional Electrophoresis To Study Differential Protein Expression in Divercin V41-Resistant and Wild-Type Strains of Listeria monocytogenes

2000 ◽  
Vol 66 (10) ◽  
pp. 4318-4324 ◽  
Author(s):  
Frederique Duffes ◽  
Paul Jenoe ◽  
Patrick Boyaval
Keyword(s):  
Transcriptional Regulation ◽  
Listeria Monocytogenes ◽  
Protein Expression ◽  
Sensitive Strain ◽  
Cell Protein ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Resistant Variant ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

ABSTRACT The use of bacteriocins from food-grade lactic acid bacteria to fight against the food-borne pathogen Listeria monocytogenes has been gaining interest. However, the emergence of resistant cells is frequently reported when Listeria is exposed to such antibacterials. A two-dimensional electrophoresis study of whole-cell protein expression of Listeria monocytogenes variants sensitive or resistant to the action of a bacteriocin produced by Carnobacterium divergens V41, divercin V41, is reported in this paper. The resistant variant obtained from the sensitive strain of L. monocytogenes P was also resistant to piscicocins V1 and SF668, but remained sensitive to nisin. Its growth rate was 50% less than the sensitive strain, and the MIC for it was 104 times higher. No reversion of the resistance was observed after 20 successive cultures in the absence of divercin V41. Comparison of the protein patterns by two-dimensional gel electrophoresis analysis showed clear differences. In the resistant variant pattern, at least nine spots had disappeared and eight new ones were observed. One of the newly synthesized proteins was identified as a flagellin of L. monocytogenes. Direct interaction between flagellin and divercin V41 was not evidenced. Intracellular synthesis of flagellin is probably an indirect effect of a modification in transcriptional regulation with widespread effects through a sigma factor. An intense protein, only present in the sensitive strain, was identified as a non-heme iron-binding ferritin displaying strong similarities to Dps proteins. Common modifications in the transcriptional regulation for these two proteins are discussed.

CHANGES IN THE TEAR PROTEIN PATTERNS OF DIABETIC PATIENTS USING TWO-DIMENSIONAL ELECTROPHORESIS.

Cornea ◽  
2000 ◽  
Vol 19 (Supplement 2) ◽  
pp. S93
Author(s):  
Simone Herber ◽  
Franz H. Grus ◽  
Perihan Sabuncuo ◽  
Albert J. Augustin
Keyword(s):  
Diabetic Patients ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Two Dimensional Electrophoresis ◽  
Tear Protein ◽  
Dimensional Electrophoresis

Clinical applications of two-dimensional electrophoresis.

1982 ◽  
Vol 28 (4) ◽  
pp. 876-883 ◽  
Author(s):  
E Jellum ◽  
A K Thorsrud
Keyword(s):  
Cerebrospinal Fluid ◽  
High Resolution ◽  
Skin Diseases ◽  
Gas Chromatography Mass Spectrometry ◽  
Two Dimensional ◽  
Blister Fluid ◽  
Protein Patterns ◽  
Two Dimensional Electrophoresis ◽  
Associated Proteins ◽  
Dimensional Electrophoresis

Abstract High-resolution two-dimensional electrophoresis has been used in our institute to study sera from patients with multiple myelomas; cerebrospinal fluid from patients with different neurological disorders; blister fluid, dermis, and epidermis from patients with skin diseases; and biopsies from brain tumors; and to search for tumor-associated proteins in cancer biopsies and pre-cancer sera. The method differentiates between all main types of immunoglobulins and gives rise to protein patterns for cerebrospinal fluid that may carry diagnostic information. The pattern of proteins in serum and blister fluid is almost identical, confirming that the latter is a filtrate of serum. We also analyzed sera collected from patients several years before it was clinically recognized that they had cancer (JANUS serum bank), in an attempt to find tumor-associated proteins in serum at an early stage of the disease. We encountered difficulties in detecting trace proteins, due to masking effects of such major serum-protein constituents as albumin. A combination of computerized gas chromatography-mass spectrometry and high-resolution two-dimensional electrophoresis is capable of mapping compounds of both low and high molecular mass. Used in combination with pattern-recognition analysis, the complete multicomponent analytical system opens the possibility of diagnosing diseased cells solely on the basis of differences in their biochemical composition.

Sialic Acid Dependent Polypeptide Chain Heterogeneity of Human Fibrinogen Demonstrated by Two-Dimensional Electrophoresis

1982 ◽  
Vol 47 (01) ◽  
pp. 019-021 ◽  
Author(s):  
Cemal Kuyas ◽  
André Haeberli ◽  
P Werner Straub
Keyword(s):  
Sialic Acid ◽  
Polypeptide Chain ◽  
Two Dimensional ◽  
Charge Heterogeneity ◽  
Human Fibrinogen ◽  
Two Dimensional Electrophoresis ◽  
Isoelectric Points ◽  
Polypeptide Chains ◽  
Dimensional Electrophoresis ◽  
Chain Type

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.

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