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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Autor principal: Mordoh, J.
Otros Autores: Krisman, C.R, Parodi, A.J, Leloir, L.F
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 1968
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
Aporte de:Registro referencial: Solicitar el recurso aquí
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008 190411s1968 xx ||||fo|||| 00| 0 eng|d
024 7 |2 scopus  |a 2-s2.0-0014424732 
024 7 |2 cas  |a acid phosphatase, 9001-77-8, 9025-88-1; amylase, 9000-90-2, 9000-92-4, 9001-19-8; sucrose, 122880-25-5, 57-50-1; Acid Phosphatase, EC 3.1.3.2; Amylases, EC 3.2.1.-; Detergents; Liver Glycogen; Sucrose, 57-50-1 
040 |a Scopus  |b spa  |c AR-BaUEN  |d AR-BaUEN 
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100 1 |a Mordoh, J. 
245 1 0 |a Some properties of rat liver amylase 
260 |c 1968 
270 1 0 |m Mordoh, J.; Instituto de Investigaciones Bioquimicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490 Buenos Aires (28), Argentina 
506 |2 openaire  |e Política editorial 
520 3 |a 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.  |l eng 
536 |a Detalles de la financiación: National Institutes of Health 
536 |a Detalles de la financiación: U.S. Public Health Service 
536 |a Detalles de la financiación: Rockefeller Foundation 
536 |a Detalles de la financiación: I This investigation was supported in part by a research grant (GM 03442) from the National Institutes of Health, U. S. Public Health Service, by the Rockefeller Foundation, and by the Consejo National de Investigaciones Cientificas y Tecnicas (R. Argentina). ’ Career investigator of the Consejo National de Investigaciones Cientiificas y Tecnicas (R. Argentina). ’ Fellow of the Consejo National de Investiga-ciones Cientificas y Tecnicas (R. Argentina). 
593 |a Instituto de Investigaciones Bioquimicas Fundación Campomar, Facultad de Ciencias Exactas y Naturales, Obligado 2490 Buenos Aires (28), Argentina 
690 1 0 |a ACID PHOSPHATASE 
690 1 0 |a AMYLASE 
690 1 0 |a DETERGENT 
690 1 0 |a SUCROSE 
690 1 0 |a ANIMAL 
690 1 0 |a ARTICLE 
690 1 0 |a BLOOD 
690 1 0 |a CELL NUCLEUS 
690 1 0 |a CYTOLOGY 
690 1 0 |a ENZYMOLOGY 
690 1 0 |a FREEZING 
690 1 0 |a GLYCOGEN LIVER LEVEL 
690 1 0 |a KINETICS 
690 1 0 |a LIVER 
690 1 0 |a LIVER MITOCHONDRION 
690 1 0 |a LYSOSOME 
690 1 0 |a METABOLISM 
690 1 0 |a MICROSOME 
690 1 0 |a RAT 
690 1 0 |a SOLUBILITY 
690 1 0 |a STIMULATION 
690 1 0 |a ACID PHOSPHATASE 
690 1 0 |a AMYLASES 
690 1 0 |a ANIMAL 
690 1 0 |a CELL NUCLEUS 
690 1 0 |a DETERGENTS 
690 1 0 |a FREEZING 
690 1 0 |a KINETICS 
690 1 0 |a LIVER 
690 1 0 |a LIVER GLYCOGEN 
690 1 0 |a LYSOSOMES 
690 1 0 |a MICROSOMES 
690 1 0 |a MITOCHONDRIA, LIVER 
690 1 0 |a RATS 
690 1 0 |a SOLUBILITY 
690 1 0 |a STIMULATION, CHEMICAL 
690 1 0 |a SUCROSE 
700 1 |a Krisman, C.R. 
700 1 |a Parodi, A.J. 
700 1 |a Leloir, L.F. 
773 0 |d 1968  |g v. 127  |h pp. 193-199  |k n. C  |p Arch. Biochem. Biophys.  |x 00039861  |w (AR-BaUEN)CENRE-1377  |t Archives of Biochemistry and Biophysics 
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856 4 0 |u https://doi.org/10.1016/0003-9861(68)90216-6  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_00039861_v127_nC_p193_Mordoh  |y Handle 
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