δ‐Aminolevulinate Dehydratase from Rat Harderian Gland Purification and Properties
δ‐Aminolevulinate dehydratase which catalyzes the second step in the biosynthesis of protoporphyrin has been purified from Harderian gland homogenates of normal rats. The enzyme preparation has a specific activity of 860 units per mg of protein at 37°, and about a 150‐fold purification from the crud...
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todo:paper_00142956_v6_n1_p84_Tomio2023-10-03T14:11:57Z δ‐Aminolevulinate Dehydratase from Rat Harderian Gland Purification and Properties Tomio, J.M. Tuzman, V. Grinstein, M. amino acid chelating agent chloride cysteine edetic acid electrolyte Hydro Lyases hydrolyase levulinic acid porphyrin sulfate thiol derivative animal article chemistry electrophoresis enzymology gel chromatography gel electrophoresis isolation and purification lacrimal apparatus nictitating membrane precipitation rat Amino Acids Animal Chelating Agents Chemistry Chlorides Chromatography, Gel Cysteine Edetic Acid Electrolytes Electrophoresis Electrophoresis, Disc Hydro-Lyases Lacrimal Apparatus Levulinic Acids Nictitating Membrane Porphyrins Precipitation Rats Sulfates Sulfhydryl Compounds δ‐Aminolevulinate dehydratase which catalyzes the second step in the biosynthesis of protoporphyrin has been purified from Harderian gland homogenates of normal rats. The enzyme preparation has a specific activity of 860 units per mg of protein at 37°, and about a 150‐fold purification from the crude extract has been achieved. The purified material appears to be homogeneous in starch gel and polyacrylamide gel disc electrophoretic studies. Partially purified enzyme preparations have an absolute requirement for cysteine or analogous thiol reagents. Effect of anions and cations is discussed. Copyright © 1968, Wiley Blackwell. All rights reserved Fil:Tomio, J.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Grinstein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00142956_v6_n1_p84_Tomio |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
amino acid chelating agent chloride cysteine edetic acid electrolyte Hydro Lyases hydrolyase levulinic acid porphyrin sulfate thiol derivative animal article chemistry electrophoresis enzymology gel chromatography gel electrophoresis isolation and purification lacrimal apparatus nictitating membrane precipitation rat Amino Acids Animal Chelating Agents Chemistry Chlorides Chromatography, Gel Cysteine Edetic Acid Electrolytes Electrophoresis Electrophoresis, Disc Hydro-Lyases Lacrimal Apparatus Levulinic Acids Nictitating Membrane Porphyrins Precipitation Rats Sulfates Sulfhydryl Compounds |
| spellingShingle |
amino acid chelating agent chloride cysteine edetic acid electrolyte Hydro Lyases hydrolyase levulinic acid porphyrin sulfate thiol derivative animal article chemistry electrophoresis enzymology gel chromatography gel electrophoresis isolation and purification lacrimal apparatus nictitating membrane precipitation rat Amino Acids Animal Chelating Agents Chemistry Chlorides Chromatography, Gel Cysteine Edetic Acid Electrolytes Electrophoresis Electrophoresis, Disc Hydro-Lyases Lacrimal Apparatus Levulinic Acids Nictitating Membrane Porphyrins Precipitation Rats Sulfates Sulfhydryl Compounds Tomio, J.M. Tuzman, V. Grinstein, M. δ‐Aminolevulinate Dehydratase from Rat Harderian Gland Purification and Properties |
| topic_facet |
amino acid chelating agent chloride cysteine edetic acid electrolyte Hydro Lyases hydrolyase levulinic acid porphyrin sulfate thiol derivative animal article chemistry electrophoresis enzymology gel chromatography gel electrophoresis isolation and purification lacrimal apparatus nictitating membrane precipitation rat Amino Acids Animal Chelating Agents Chemistry Chlorides Chromatography, Gel Cysteine Edetic Acid Electrolytes Electrophoresis Electrophoresis, Disc Hydro-Lyases Lacrimal Apparatus Levulinic Acids Nictitating Membrane Porphyrins Precipitation Rats Sulfates Sulfhydryl Compounds |
| description |
δ‐Aminolevulinate dehydratase which catalyzes the second step in the biosynthesis of protoporphyrin has been purified from Harderian gland homogenates of normal rats. The enzyme preparation has a specific activity of 860 units per mg of protein at 37°, and about a 150‐fold purification from the crude extract has been achieved. The purified material appears to be homogeneous in starch gel and polyacrylamide gel disc electrophoretic studies. Partially purified enzyme preparations have an absolute requirement for cysteine or analogous thiol reagents. Effect of anions and cations is discussed. Copyright © 1968, Wiley Blackwell. All rights reserved |
| format |
JOUR |
| author |
Tomio, J.M. Tuzman, V. Grinstein, M. |
| author_facet |
Tomio, J.M. Tuzman, V. Grinstein, M. |
| author_sort |
Tomio, J.M. |
| title |
δ‐Aminolevulinate Dehydratase from Rat Harderian Gland Purification and Properties |
| title_short |
δ‐Aminolevulinate Dehydratase from Rat Harderian Gland Purification and Properties |
| title_full |
δ‐Aminolevulinate Dehydratase from Rat Harderian Gland Purification and Properties |
| title_fullStr |
δ‐Aminolevulinate Dehydratase from Rat Harderian Gland Purification and Properties |
| title_full_unstemmed |
δ‐Aminolevulinate Dehydratase from Rat Harderian Gland Purification and Properties |
| title_sort |
δ‐aminolevulinate dehydratase from rat harderian gland purification and properties |
| url |
http://hdl.handle.net/20.500.12110/paper_00142956_v6_n1_p84_Tomio |
| work_keys_str_mv |
AT tomiojm daminolevulinatedehydratasefromratharderianglandpurificationandproperties AT tuzmanv daminolevulinatedehydratasefromratharderianglandpurificationandproperties AT grinsteinm daminolevulinatedehydratasefromratharderianglandpurificationandproperties |
| _version_ |
1807322745238716416 |