scholarly journals Genetic diversity analysis of faba bean (Vicia faba L.) germplasms using sodium dodecyl sulfate-polyacrylamide gel electrophoresis

2015 ◽  
Vol 14 (4) ◽  
pp. 13945-13953 ◽  
Author(s):  
W.W. Hou ◽  
X.J. Zhang ◽  
J.B. Shi ◽  
Y.J. Liu
Keyword(s):  
Genetic Diversity ◽  
Sodium Dodecyl Sulfate ◽  
Vicia Faba ◽  
Faba Bean ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Diversity Analysis ◽  
Genetic Diversity Analysis ◽  
Vicia Faba L

Genetic Diversity Analysis of Faba Bean (Vicia faba L.) Based on EST-SSR Markers

2011 ◽  
Vol 10 (6) ◽  
pp. 838-844 ◽  
Author(s):  
Ya-ming GONG ◽  
Sheng-chun XU ◽  
Wei-hua MAO ◽  
Ze-yun LI ◽  
Qi-zan HU ◽  
...  
Keyword(s):  
Genetic Diversity ◽  
Vicia Faba ◽  
Ssr Markers ◽  
Faba Bean ◽  
Diversity Analysis ◽  
Genetic Diversity Analysis ◽  
Vicia Faba L

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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