Two-dimensional Electrophoresis of the α-Chains of Collages and Its Application to the Determination of their Isoelectric Points

1981 ◽  
Vol 1 (3) ◽  
pp. 237-246 ◽  
Author(s):  
Shizuko Tanaka ◽  
Ryu-Ichiro Hata ◽  
Yutaka Nagai
Keyword(s):  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Isoelectric Points ◽  
Dimensional Electrophoresis

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.

Analytical electrofocusing and two-dimensional electrophoresis of proteins extracted from the mycelia of aggressive and nonaggressive strains of Ophiostoma ulmi

1986 ◽  
Vol 64 (9) ◽  
pp. 2073-2081 ◽  
Author(s):  
Robert S. Jeng
Keyword(s):  
Dutch Elm Disease ◽  
Two Dimensional ◽  
Polyacrylamide Gels ◽  
Ophiostoma Ulmi ◽  
Two Dimensional Electrophoresis ◽  
Coomassie Blue ◽  
Isoelectric Points ◽  
Additional Protein ◽  
Dimensional Electrophoresis ◽  
Electrophoresis Of Proteins

Soluble mycelial proteins from Ophiostoma ulmi (Buism.) Nannf., the causal agent of Dutch elm disease, were separated by analytical electrofocusing and two-dimensional electrophoresis in polyacrylamide gels. Results showed the aggressive and nonaggressive strains of this pathogen each had about 60 Coomassie blue stained bands having isoelectric points from 3 to 7. Both strains of this fungus had their own characteristic electrofocusing patterns. Nonaggressive isolate S116, for example, lacked two protein bands, one near the anode and one near the cathode, but it had five additional protein bands distributed from pH 4 to 6. Two-dimensional electrophoresis of total soluble proteins depicted that there were 36 proteins found to be specific for the nonaggressive isolate S116 and 12 proteins for the aggressive isolate RR2.

Plasma apolipoproteins in Tangier disease, as studied with two-dimensional electrophoresis.

1987 ◽  
Vol 33 (1) ◽  
pp. 120-122 ◽  
Author(s):  
S Visvikis ◽  
M F Dumon ◽  
J Steinmetz ◽  
T Manabe ◽  
M M Galteau ◽  
...  
Keyword(s):  
The Other ◽  
High Density Lipoproteins ◽  
Major Protein ◽  
Two Dimensional ◽  
Tangier Disease ◽  
Two Dimensional Electrophoresis ◽  
Isoelectric Points ◽  
Molecular Masses ◽  
Dimensional Electrophoresis ◽  
Homozygous Patient

Abstract Tangier disease is characterized by a deficiency of high-density lipoproteins and of their major protein constituent, apolipoprotein (apo) A-I. We used high-resolution two-dimensional electrophoresis to examine the principal plasma apolipoproteins (A-I, A-II, A-IV, E, C-II, and C-III) of three persons with Tangier disease, one homozygous patient and his two heterozygous children, comparing the patterns with those for healthy subjects. Characteristic abnormalities were found in the distribution of the isoproteins of apo A-I, there being a normal concentration of pro apo A-I but dramatically decreased concentrations of the other apo A-I isoproteins. We also found hitherto-undescribed polypeptide abnormalities in apo C-III: sialylated and nonsialylated forms of apo C-III appear as double spots having the same isoelectric points but different molecular masses. No other substantial difference was detected in the polypeptide distribution of the other plasma apolipoproteins.

scholarly journals AUTOMATIC SELECTION OF TWO-DIMENSIONAL ELECTROPHORESIS GEL WITH LEAST GEOMETRIC DISTORTIONS

2010 ◽  
Vol 2 (1) ◽  
pp. 9-13
Author(s):  
Dalius Matuzevičius
Keyword(s):  
Quality Criterion ◽  
Horizontal Line ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Two Dimensional Electrophoresis ◽  
Geometric Distortions ◽  
Biochemical Experiment ◽  
Dimensional Electrophoresis ◽  
Selection Of

The paper presents an algorithm for automated selection of the highest quality two-dimensional gel electrophoresis image. The quality criterion is the amount of vertical geometric distortions of the gel. The aim is to select the least distorted gel from the group received during the same biochemical experiment. Vertical geometric distortions displace proteins of the same molecular mass from the horizontal line and have a greater impact on the determination of protein characteristics than horizontal distortions. After presenting algorithm for evaluation of distortions and selection of base gel results are compared to expert's made selections. If necessary, algorithm may be adapted for horizontal distortion evaluation.

The oral apparatus of Tetrahymena. V. Oral apparatus polypeptides and their distribution

1980 ◽  
Vol 44 (1) ◽  
pp. 317-333
Author(s):  
R.H. Gavin
Keyword(s):  
Molecular Weight ◽  
Basal Body ◽  
Tetrahymena Thermophila ◽  
Electrophoretic Analysis ◽  
Two Dimensional ◽  
Molecular Weight Range ◽  
Two Dimensional Electrophoresis ◽  
Weight Range ◽  
Isoelectric Points ◽  
Dimensional Electrophoresis

Two-dimensional electrophoresis was used to resolve approximately 162 polypeptides from the isolated oral apparatus of Tetrahymena thermophila. The molecular weight range was between 110 000 and 15 000 Daltons. The polypeptides had apparent isoelectric points between pH 3.3 and pH 7.2. Electrophoretic analysis of isolated ciliary axonemes and fractionated oral apparatuses made possible the assignment of polypeptides to structures within the oral apparatus. Approximately 24 polypeptides, including alpha and beta tubulins, are probable components of the basal body-basal plate complex. At least 5 of the oral apparatus polypeptides, including alpha and beta tubulin, are components of the oral apparatus ciliary axonemes. Approximately 138 polypeptides are components of the oral apparatus framework.

Quantitative determination of haptoglobin glycoform variants in psoriasis

2010 ◽  
Vol 391 (12) ◽  
Author(s):  
Bernardetta Maresca ◽  
Luisa Cigliano ◽  
Maria M. Corsaro ◽  
Giuseppina Pieretti ◽  
Massimo Natale ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Immune Response ◽  
Extracellular Matrix ◽  
Quantitative Determination ◽  
Glycan Structure ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Plasma Haptoglobin

AbstractHaptoglobin is an acute phase glycoprotein, secreted by hepatocytes and other types of cells including keratinocytes. Haptoglobin has been suggested to impair the immune response, inhibit gelatinases in the extracellular matrix and promote angiogenesis, but its role in psoriasis is obscure to date. Changes in haptoglobin glycan structure were observed in several diseases. The aim of this study was to investigate whether haptoglobin displays glycan variations in psoriasis. We found that the pattern of plasma haptoglobin glycoforms, following two-dimensional electrophoresis, exhibited significant quantitative differences in spot intensities between patients and controls. Quantitative and qualitative differences in glycan mass, between patients and controls, were found by mass spectrometry of glycopeptides from tryptic digests of protein isolated from both patients and controls. The number of distinct fucosylated glycoforms of peptides NLFLNHSENATAK and MVSHHNLTTGATLINEQWLLTTAK was higher in patients than in controls, but no fucosylated glycan was detected on peptide VVLHPNYSQ-VDIGLIK in either case. The number of peptides with distinct triantennary and tetraantennary glycans was higher in patients than in controls. Abundance or structure of specific glycans, which are present in haptoglobin from patients and are different or missing in normal haptoglobin, might be associated with disease activity.

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