Prenatal diagnosis of mucopolysaccharidosis by two-dimensional electrophoresis of amniotic fluid glycosaminoglycans

1982 ◽  
Vol 2 (3) ◽  
pp. 169-176 ◽  
Author(s):  
Jean Mossman ◽  
A. D. Patrick
Keyword(s):  
Prenatal Diagnosis ◽  
Amniotic Fluid ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

Proteins of human amniotic fluid. II. Mapping by two-dimensional electrophoresis.

1982 ◽  
Vol 28 (4) ◽  
pp. 935-940 ◽  
Author(s):  
P Burdett ◽  
J Lizana ◽  
P Eneroth ◽  
K Bremme
Keyword(s):  
Amniotic Fluid ◽  
Molecular Mass ◽  
Staining Technique ◽  
Two Dimensional ◽  
Human Amniotic Fluid ◽  
Two Dimensional Electrophoresis ◽  
Electrophoretic Techniques ◽  
Silver Staining Technique ◽  
Dimensional Electrophoresis ◽  
Blue Sepharose

Abstract In an earlier study we used various electrophoretic techniques to investigate the proteins in amniotic fluid, including two-dimensional electrophoresis. However, the high proportion of albumin dominated the pattern and tended to distort the pH gradient. Improved methodology, based upon the removal of albumin with Blue Sepharose CL6B and the silver-staining technique, has been used in the present work. These modifications have minimized problems of distortion. We have extended our work in a attempt to complete the two-dimensional map of the proteins in amniotic fluid. Over 200 proteins were seen, ranging in molecular mass from 10 000 to 100 000, including a relatively high proportion of polypeptides of low-molecular mass. The spots seen in the map are discussed in relation to some of the proteins, peptides, and hormones that have been reported in amniotic fluid. Eventually, it is hoped that polypeptides will be found that will provide better indicators of the condition of the fetus.

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.

Improvement of Two-dimensional Electrophoresis of Rice (Oryza sativaL.) Proteomics

2012 ◽  
Vol 18 (5) ◽  
pp. 819 ◽  
Author(s):  
Yanhua YANG ◽  
Weitong CUI ◽  
Xiaoyong LIU ◽  
Keming ZHU ◽  
Keping CHEN
Keyword(s):  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis
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