scholarly journals Two-dimensional electrophoresis of plasma membranes, showing differences among wild-type and abnormal ascospore mutant strains of Neurospora crassa.

1983 ◽  
Vol 155 (3) ◽  
pp. 1393-1398 ◽  
Author(s):  
J B Nasrallah ◽  
A M Srb
Keyword(s):  
Neurospora Crassa ◽  
Plasma Membranes ◽  
Two Dimensional ◽  
Wild Type ◽  
Two Dimensional Electrophoresis ◽  
Mutant Strains ◽  
Dimensional Electrophoresis

Alterations in the pattern of polypeptide synthesis resulting from amino acid limitation in Neurospora crassa

1988 ◽  
Vol 34 (10) ◽  
pp. 1166-1170 ◽  
Author(s):  
Harry J. Flint ◽  
Janis McKormick
Keyword(s):  
Amino Acid ◽  
Neurospora Crassa ◽  
Two Dimensional ◽  
Wild Type ◽  
Supply Rate ◽  
Limited Growth ◽  
Synthetic Enzymes ◽  
Two Dimensional Electrophoresis ◽  
Polypeptide Synthesis ◽  
Dimensional Electrophoresis

Two-dimensional electrophoresis was used to examine the pattern of polypeptide synthesis in Neurospora crassa mycelium of an arg-6 strain grown in the presence of [14C]arginine. Reduction in the arginine supply rate led to amino acid limited growth, and to major alterations in the pattern of polypeptide synthesis. Strains carrying wild-type (cpc-1+) or mutant (cpc-1) alleles at a locus governing cross-pathway control of amino acid synthetic enzymes differed markedly with respect to their pattern of polypeptide synthesis under limitation conditions, but differed little during arginine sufficient growth. Among 160 abundant polypeptide species classified for their response to limitation in two dimensional fluorographs, 31 were induced by limitation only in a cpc-1+ strain, 13 only in a cpc-1 strain, and 9 showed induction in both strains.

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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