Purification and partial characterization of glyceraldehyde-phosphate dehydrogenase from electric organ of Electrophorus electricus (L.).
Z Naturforsch C J Biosci
; 53(5-6): 416-20, 1998.
Article
em En
| MEDLINE
| ID: mdl-9679332
The glyceraldehyde-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) was purified to homogeneity from electric organ of Electrophorus electricus (L.) by a hydrophobic chromatography 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 isoelectrophocusing 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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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Órgão Elétrico
/
Gliceraldeído-3-Fosfato Desidrogenases
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Z Naturforsch C J Biosci
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Brasil
País de publicação:
Alemanha