scholarly journals Heterogeneity of the molecular defect in human dihydropteridine reductase deficiency

1981 ◽  
Vol 198 (3) ◽  
pp. 677-682 ◽  
Author(s):  
F A Firgaira ◽  
K H Choo ◽  
R G H Cotton ◽  
D M Danks
Keyword(s):  
Affinity Chromatography ◽  
Gel Electrophoresis ◽  
Cultured Cells ◽  
Mutant Gene ◽  
Mutant Enzyme ◽  
Molecular Defect ◽  
Two Dimensional ◽  
Dihydropteridine Reductase ◽  
Two Dimensional Gel Electrophoresis ◽  
Reductase Deficiency

Radioimmunoassay, immunoprecipitation, affinity chromatography and two-dimensional gel electrophoresis were used to test cultured cells from three families with dihydropteridine reductase deficiency for a catalytically incompetent product of the mutant gene. No mutant enzyme was detected in one dihydropteridine reductase-deficient homozygote or in her parents. A second homozygote and both her parents had easily detectable concentrations of inactive mutant enzyme. In a third family one parent fitted into each of these categories.

A New Genetic Fibrinogen Variant (Fibrinogen Erfurt I) Structurally Characterized by an Abnormal Bβ-Chain and Present both in Plasma and Platelets

1988 ◽  
Vol 59 (02) ◽  
pp. 138-142 ◽  
Author(s):  
M Meyer ◽  
I Schellenberg ◽  
G Vogel ◽  
I Bischoff
Keyword(s):  
High Resolution ◽  
Gel Electrophoresis ◽  
Blood Platelets ◽  
Mutant Gene ◽  
Molecular Defect ◽  
Heterozygous State ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Asymptomatic Woman ◽  
Molecular Abnormality

SummaryAn abnormal fibrinogen was discovered in the plasma of a clinically asymptomatic woman. This fibrinogen variant was analyzed by high resolution two–dimensional gel electrophoresis and its molecular abnormality established consisting in a slight decrease in molecular mass of the Bβ–chains. Analysis of fibrin revealed that cleavage of fibrinopeptide B by thrombin is normal, the molecular defect being confined to the β–portion of the Bβ–chain. The same fibrinogen variant was detected in the blood platelets of the proposita. This finding supports the assumption of a common origin of plasma and platelet fibrinogen pools. Family studies revealed the presence of the abnormal fibrinogen in a brother of the proposita, thus confirming the genetic nature of the observed variant. The underlying mutant gene occurs in both carriers in heterozygous state.

scholarly journals Identification of Proteins Related to Nickel Homeostasis in Helicobater pylori by Immobilized Metal Affinity Chromatography and Two-Dimensional Gel Electrophoresis

2008 ◽  
Vol 2008 ◽  
pp. 1-6 ◽  
Author(s):  
Xuesong Sun ◽  
Ruiguang Ge ◽  
Jen-Fu Chiu ◽  
Hongzhe Sun ◽  
Qing-Yu He
Keyword(s):  
Affinity Chromatography ◽  
Gel Electrophoresis ◽  
Interacting Proteins ◽  
Peptic Ulcers ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Iron Storage ◽  
Cell Extracts ◽  
Nickel Homeostasis ◽  
H Pylori

Helicobacter pylori (H. pylori) is a widespread human pathogen causing peptic ulcers and chronic gastritis. Maintaining nickel homeostasis is crucial for the establishment of H. pylori infection in humans. We used immobilized-nickel affinity chromatography to isolate Ni-related proteins from H. pylori cell extracts. Two-dimensional gel electrophoresis and mass spectrometry were employed to separate and identify twenty two Ni-interacting proteins in H. pylori. These Ni-interacting proteins can be classified into several general functional categories, including cellular processes (HspA, HspB, TsaA, and NapA), enzymes (Urease, Fumarase, GuaB, Cad, PPase, and DmpI), membrane-associated proteins (OM jhp1427 and HpaA), iron storage protein (Pfr), and hypothetical proteins (HP0271, HP jhp0216, HP jhp0301, HP0721, HP0614, and HP jhp0118). The implication of these proteins in nickel homeostasis is discussed.

Further characterization of the posttranslational modifications of core histones in response to heat and arsenite stress in Drosophila

1986 ◽  
Vol 64 (8) ◽  
pp. 750-757 ◽  
Author(s):  
Richard Desrosiers ◽  
Robert M. Tanguay
Keyword(s):  
Heat Shock ◽  
Posttranslational Modifications ◽  
Gel Electrophoresis ◽  
Cultured Cells ◽  
Histone Variants ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Nonhistone Protein ◽  
The Core ◽  
Core Histones

The effects of a heat shock or arsenite treatment on the methylation and acetylation of core histones have been investigated in Drosophila cultured cells. The decrease in H3 methylation, which is observed during a heat shock, is not a demethylation process, but results from methylation arrest. Two-dimensional gel electrophoresis leaves no ambiguity concerning the identity of H2B as a methylated protein, since H2B and D2, a nuclear nonhistone protein, which comigrate on one-dimensional gels, are well separated on these gels. Two-dimensional gel electrophoresis in the presence of Triton X-100 resolves each of the core histones into multiple forms resulting from posttranslational modifications. There are apparently, however, no histone variants in cultured Drosophila cells. At 23 °C, the various forms of the core histones resolved on two-dimensional gels are methylated. Under heat-shock or arsenite treatment, the methylation of all forms of H3 is decreased, while that of the various forms of H2B increases. These stress conditions also induce a generalized diminution in the acetylation of all forms of core histones. In the course of a heat shock, the synthesis of H2B is increased and this newly synthesized histone remains unacetylated during the shock. These changes in the patterns of core histone methylation and acetylation may be correlated with the reorganization of gene activity brought about by the heat shock.

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