Some properties of rat liver amylase
Some properties of rat liver amylase were studied. It was confirmed that this enzyme is located mainly in the microsomal fraction and that it is activated by detergents. The effects of digitonin, Triton X-100 and sodium deoxycholate on the amylase were compared. It was observed that amylase requires...
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1968
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v127_nC_p193_Mordoh http://hdl.handle.net/20.500.12110/paper_00039861_v127_nC_p193_Mordoh |
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paper:paper_00039861_v127_nC_p193_Mordoh2023-06-08T14:24:54Z Some properties of rat liver amylase Krisman de Fischman, Clara Rebeca Parodi, Armando José acid phosphatase amylase detergent sucrose animal article blood cell nucleus cytology enzymology freezing glycogen liver level kinetics liver liver mitochondrion lysosome metabolism microsome rat solubility stimulation Acid Phosphatase Amylases Animal Cell Nucleus Detergents Freezing Kinetics Liver Liver Glycogen Lysosomes Microsomes Mitochondria, Liver Rats Solubility Stimulation, Chemical Sucrose Some properties of rat liver amylase were studied. It was confirmed that this enzyme is located mainly in the microsomal fraction and that it is activated by detergents. The effects of digitonin, Triton X-100 and sodium deoxycholate on the amylase were compared. It was observed that amylase requires a higher concentration of Triton X-100 for maximal activation than lysosomal acid phosphatase. When lysosomes and microsomes were submitted to a detergent treatment capable of activating completely acid phosphatase and α-amylase, the former was solubilized, while the second remained particulate. The activation of α-amylase was found to be reversible in the first stages. The microsomal α-amylase is not bound to glycogen in fed rats. It was observed that the free α-amylase did not change when the liver was induced to accumulate different amounts of glycogen by administration of sugar, but that latent amylase was doubled when large amounts of glycogen accumulated. The Km of liver amylase for glycogen is 2.5 mg/ml as compared with 0.4 mg/ml for serum amylase. The significance of these observations is discussed. © 1968. Fil:Krisman, C.R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Parodi, A.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1968 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v127_nC_p193_Mordoh http://hdl.handle.net/20.500.12110/paper_00039861_v127_nC_p193_Mordoh |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
acid phosphatase amylase detergent sucrose animal article blood cell nucleus cytology enzymology freezing glycogen liver level kinetics liver liver mitochondrion lysosome metabolism microsome rat solubility stimulation Acid Phosphatase Amylases Animal Cell Nucleus Detergents Freezing Kinetics Liver Liver Glycogen Lysosomes Microsomes Mitochondria, Liver Rats Solubility Stimulation, Chemical Sucrose |
| spellingShingle |
acid phosphatase amylase detergent sucrose animal article blood cell nucleus cytology enzymology freezing glycogen liver level kinetics liver liver mitochondrion lysosome metabolism microsome rat solubility stimulation Acid Phosphatase Amylases Animal Cell Nucleus Detergents Freezing Kinetics Liver Liver Glycogen Lysosomes Microsomes Mitochondria, Liver Rats Solubility Stimulation, Chemical Sucrose Krisman de Fischman, Clara Rebeca Parodi, Armando José Some properties of rat liver amylase |
| topic_facet |
acid phosphatase amylase detergent sucrose animal article blood cell nucleus cytology enzymology freezing glycogen liver level kinetics liver liver mitochondrion lysosome metabolism microsome rat solubility stimulation Acid Phosphatase Amylases Animal Cell Nucleus Detergents Freezing Kinetics Liver Liver Glycogen Lysosomes Microsomes Mitochondria, Liver Rats Solubility Stimulation, Chemical Sucrose |
| description |
Some properties of rat liver amylase were studied. It was confirmed that this enzyme is located mainly in the microsomal fraction and that it is activated by detergents. The effects of digitonin, Triton X-100 and sodium deoxycholate on the amylase were compared. It was observed that amylase requires a higher concentration of Triton X-100 for maximal activation than lysosomal acid phosphatase. When lysosomes and microsomes were submitted to a detergent treatment capable of activating completely acid phosphatase and α-amylase, the former was solubilized, while the second remained particulate. The activation of α-amylase was found to be reversible in the first stages. The microsomal α-amylase is not bound to glycogen in fed rats. It was observed that the free α-amylase did not change when the liver was induced to accumulate different amounts of glycogen by administration of sugar, but that latent amylase was doubled when large amounts of glycogen accumulated. The Km of liver amylase for glycogen is 2.5 mg/ml as compared with 0.4 mg/ml for serum amylase. The significance of these observations is discussed. © 1968. |
| author |
Krisman de Fischman, Clara Rebeca Parodi, Armando José |
| author_facet |
Krisman de Fischman, Clara Rebeca Parodi, Armando José |
| author_sort |
Krisman de Fischman, Clara Rebeca |
| title |
Some properties of rat liver amylase |
| title_short |
Some properties of rat liver amylase |
| title_full |
Some properties of rat liver amylase |
| title_fullStr |
Some properties of rat liver amylase |
| title_full_unstemmed |
Some properties of rat liver amylase |
| title_sort |
some properties of rat liver amylase |
| publishDate |
1968 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v127_nC_p193_Mordoh http://hdl.handle.net/20.500.12110/paper_00039861_v127_nC_p193_Mordoh |
| work_keys_str_mv |
AT krismandefischmanclararebeca somepropertiesofratliveramylase AT parodiarmandojose somepropertiesofratliveramylase |
| _version_ |
1768544710260948992 |