glyceraldehyde phosphate dehydrogenase
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2010 ◽  
Vol 60 (9) ◽  
pp. 2236-2246 ◽  
Author(s):  
Lenka Zídková ◽  
Ivan Cepicka ◽  
Jan Votýpka ◽  
Milena Svobodová

Monoxenous trypanosomatid Herpetomonas trimorpha sp. nov. was isolated from the digestive tract of the biting midge Culicoides truncorum (Ceratopogonidae, Diptera). This species forms three distinct morphotypes in culture: the microflagellate promastigote, the small promastigote and the long promastigote. The last form is unique for the newly described species. Phylogenetic analyses of SSU rRNA and glycosomal glyceraldehyde phosphate dehydrogenase genes showed that H. trimorpha sp. nov. is the closest relative of Herpetomonas ztiplika, another monoxenous trypanosomatid isolated from biting midges. However, morphological and randomly amplified polymorphic DNA analyses confirmed that H. trimorpha sp. nov. is distinct from H. ztiplika.


2004 ◽  
Vol 34 (12) ◽  
pp. 1393-1404 ◽  
Author(s):  
Patrick B. Hamilton ◽  
Jamie R. Stevens ◽  
Michael W. Gaunt ◽  
Jennifer Gidley ◽  
Wendy C. Gibson

2002 ◽  
Vol 34 (11) ◽  
pp. 1549-1560 ◽  
Author(s):  
Philip Eaton ◽  
Neville Wright ◽  
David J. Hearse ◽  
Michael J. Shattock

1998 ◽  
Vol 53 (5-6) ◽  
pp. 416-420 ◽  
Author(s):  
S. Giovanni-De-Simone ◽  
A. Hassón-Voloch ◽  
C. Batista-e-Silva ◽  
A. Nery-da-Matta

Abstract The glyceraldehyde-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) was purified to homogeneity from electric organ of Electrophorus electricus (L.) by a hydrophobic chroma­ tography method on deacetylcolchicine-Sepharose. The purification resulted in a 162 fold increase in specific activity of the GAPDH and final yield was approximately 37%. The purified enzyme showed a single band in SDS-PAGE, with an apparent molecular mass of 36 kDa. The purity of the colchicine-Sepharose isolated material was analysed by isoelectro-phocusing and immunoblotting using a heterologous rabbit serum anti-GAPDH. Sequence analysis of the 40-N-terminal amino acids, determined by Edman degradation, revealed its identity to other GAPDHs proteins being the largest number of identical amino acids to lobster (92.5%), rabbit muscle (85%) and human liver (80%) GAPDH.


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