Go toArchive
Browse byFacets
Bookbag ( 0 )
'Hydrophobic Chromatography' in keywords
Results  2 Items
Sorted by   
Publication Year
1998 (1)
1987 (1)
1Author    Pedro Macias, M., Carmen Pinto, JoseE. CampilloRequires cookie*
 Title    Purification and Partial Characterization of Rat Liver Lipoxygenase  
 Abstract    Lipoxygenase was purified from rat liver cytosolic fraction by a method involving two successive chromatographic steps on Sephacryl S-200 and Phenyl Sepharose CL-4B. The enzyme has a molecular weight of 96 Kdal and it seems to be composed of two identical subunits. Chromatofocusing of the enzyme revealed a single band of activity at pi 6.3. The enzyme activity of the purified fraction showed maximum activity at pH 7.0 with a Km for linoleic acid of 1.4 /<M and is competitively inhibited by the specific lipoxygenase inhibitor nordihydroguaiaretic acid. The purified enzyme shows absorption and fluorescence spectra similar to those of lipoxygenase from other sources. However, the molecular weight of lipoxygenase purified from liver is found to be different from that of the enzyme from polymorphonuclear leukocytes. It is suggested that there are different isoenzymes of lipoxygenases in mammals. 
  Reference    Z. Naturforsch. 42b, 1343—1348 (1987); received March 16 1987 
  Published    1987 
  Keywords    Lipoxygenase, Enzyme Purification, Hydrophobic Chromatography 
  Similar Items    Find
 TEI-XML for    default:Reihe_B/42/ZNB-1987-42b-1343.pdf 
 Identifier    ZNB-1987-42b-1343 
 Volume    42 
2Author    S. Giovanni-De-Simonea, A. Hassón-Volochc, C. Batista, -E-Silvac, A. Nery, -Da-M AttaaRequires cookie*
 Title    Purification and Partial Characterization of Glyceraldehyde-Phosphate Dehydrogenase from Electric Organ of Electrophorus electricus (L.)  
 Abstract    The glyceraldehyde-phosphate dehydrogenase (GAPDH, EC 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. 
  Reference    Z. Naturforsch. 53c, 416—420 (1998); received November 11 1997 
  Published    1998 
  Keywords    Electrophorus electricus (L), Glyceraldehyde-phosphate Dehydrogenase, Glycolytic Enzyme, Hydrophobic Chromatography, NH2-Terminal Sequence 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/53/ZNC-1998-53c-0416.pdf 
 Identifier    ZNC-1998-53c-0416 
 Volume    53