| | 1 | Author
| Pedro Macias, M., Carmen Pinto, JoseE. Campillo | Requires 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 | | | |
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| default:Reihe_B/42/ZNB-1987-42b-1343.pdf | | | | Identifier
| ZNB-1987-42b-1343 | | | | Volume
| 42 | |
| 2 | Author
| S. Giovanni-De-Simonea, A. Hassón-Volochc, C. Batista, -E-Silvac, A. Nery, -Da-M Attaa | Requires cookie* | | | Title
| Purification and Partial Characterization of Glyceraldehyde-Phosphate Dehydrogenase from Electric Organ of Electrophorus electricus (L.) | | | | 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. | | | |
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 | | | |
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| default:Reihe_C/53/ZNC-1998-53c-0416.pdf | | | | Identifier
| ZNC-1998-53c-0416 | | | | Volume
| 53 | |
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