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The Assay of Catalases and Peroxidases
Abstract
Publisher Summary This chapter discusses the assay of catalases and peroxidases are: (1) catalase assay by disappearance of peroxide; (2) method for crude cell extracts; (3) direct spectrophotometric assay of catalase and peroxidase in cells and tissues; and (4) peroxidase assay by spectrophotometric measurements of the disappearance of hydrogen donor or the appearance of their colored oxidation products. Two methods are described for the catalase assay by disappearance of peroxide are: ultraviolet spectrophotometry and permanganate titration. Ultraviolet spectrophotometryis a method devised, on the basis of the absorption curves for peroxide solutions, for determining the activity of catalase by direct measurements of the decrease of light absorption in the region 230 to 250 mμ caused by the decomposition of hydrogen peroxide by catalase. In the case of method for crude cell extracts, oxygen evolution caused by the decomposition of hydrogen peroxide is measured with the conventional manometric technique. Peroxidase assay by spectrophotometric measurements of the disappearance of hydrogen donor or the appearance of their colored oxidation products includes the guaiacol test and the pyrogallol test.
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Research works printed but not linked: 413
- Chance B., 1951, Advances in Enzymology, 153
- Chance B., 1951, The Enzymes, 428
- Chance B., 1952, Modern Trends in Biochemistry and Physiology, 25
- Chance B., 1953, Investigation of Rates and Mechanisms of Reactions, 627
- 10.1146/annurev.bi.21.070152.003351 · doi:10.1146/annurev.bi.21.070152.003351
- George P., 1953, Advances in Catalysis, 367
- 10.1042/bj0490088 · DOI · Paper page
- Lemberg R., 1949, Hematin Compounds and Bile Pigments, Their Constitution, Metabolism, and Function.
- Maehly A. C., 1950, “Vom Stand der Peroxydaseforschung,”, Z. Vitamin‐. Hormon‐, und Fermentforsch., 3, 115
- Theorell H., 1943, “Einige neue Untersuchungen über Cytochrome, Peroxidasen und Katalasen,”, Ergeb. Enzymforsch., 9, 231
- Theorell H., 1947, Advances in Enzymology, 265
- Theorell H., 1951, The Enzymes, 397
- Wyman Jeffries, 1948, Advances in Protein Chemistry, 407
- Abelous J. D., 1899, Compt. rend. soc. biol, 51, 328
- 10.1016/S0021-9258(18)72725-7 · DOI
- 10.1038/bjc.1950.18 · doi:10.1038/bjc.1950.18
- 10.1515/bchm2.1904.41.1-2.59 · doi:10.1515/bchm2.1904.41.1-2.59
- 10.1042/bj0321702 · doi:10.1042/bj0321702
- Agner K., 1941, Acta Physiol. Scand., 2
- Agner K., 1942, Arkiv Kemi Mineral. Geol., 16
- Agner K., 1946, Arch. Biochem., 10, 321
- 10.1515/bchm2.1933.218.1-2.113 · doi:10.1515/bchm2.1933.218.1-2.113
- Alliot H., 1902, Ann. chim. anal. chim. appl., 7, 210
- Altschul A. M., 1939, J. Biol. Chem., 130, 427, 10.1016/S0021-9258(18)73598-9 · doi:10.1016/s0021-9258(18)73598-9
- 10.1016/S0021-9258(18)73036-6 · DOI
- Altschul A. M., 1947, Arch. Biochem., 13, 161
- Alvarez M. C., 1918, Am. J. Physiol., 46, 186, 10.1152/ajplegacy.1918.46.3.186 · doi:10.1152/ajplegacy.1918.46.3.186
- Amberg S., 1911, J. Biol. Chem., 10, 295, 10.1016/S0021-9258(18)88793-2 · doi:10.1016/s0021-9258(18)88793-2
- Anan K., 1951, J. Biochem. (Japan), 38, 19
- Appleman C. O., 1910, Botan. Gaz., 50, 182, 10.1086/330309 · doi:10.1086/330309
- 10.1002/j.1537-2197.1918.tb05495.x · doi:10.1002/j.1537-2197.1918.tb05495.x
- 10.1021/ac60059a026 · doi:10.1021/ac60059a026
- Atami S., 1950, Igaku to Seibutsugaku (Med. and Biol.), 16, 68
- 10.3891/acta.chem.scand.07-0444 · doi:10.3891/acta.chem.scand.07-0444
- 10.2307/2435197 · doi:10.2307/2435197
- 10.1002/cber.190503802112 · doi:10.1002/cber.190503802112
- 10.1002/cber.190203502228 · doi:10.1002/cber.190203502228
- 10.1002/cber.190303601119 · DOI
- 10.1002/cber.19040370222 · doi:10.1002/cber.19040370222
- Bach A., 1930, Biochem. Z., 226, 482
- Bach A., 1921, Biochem. Z., 125, 283
- Bach E., 1922, Z. klin. Med., 95, 88
- Bailey C. H., 1917, J. Biol. Chem., 32, 539, 10.1016/S0021-9258(18)86638-8 · doi:10.1016/s0021-9258(18)86638-8
- Balls A. K., 1932, J. Assoc. Official Agr. Chemists, 15, 483
- Balls A. K., 1933, J. Assoc. Official Agr. Chemists, 16, 445
- 10.1042/bj0281911 · doi:10.1042/bj0281911
- 10.1515/bchm2.1926.157.4-6.192 · doi:10.1515/bchm2.1926.157.4-6.192
- Barbieri P., 1912, Biochem. Z., 42, 137
- 10.1039/jr9480000116 · doi:10.1039/jr9480000116
- Batelli F., 1905, Arch. fisiol., 2, 471
- Batelli F., 1908, Biochem. Z., 13, 44
- 10.1007/BF02325441 · doi:10.1007/bf02325441
- Becht F. C., 1919, Am. J. Physiol., 48, 171, 10.1152/ajplegacy.1919.48.2.171 · doi:10.1152/ajplegacy.1919.48.2.171
- 10.1021/ie50354a025 · DOI
- 10.1016/S0021-9258(19)50881-X · DOI · Paper page
- 10.1126/science.117.3052.710-a · doi:10.1126/science.117.3052.710-a
- 10.1007/BF01687441 · doi:10.1007/bf01687441
- Bertrand G., 1897, Ann. chim. phys., 12, 115
- Bertrand G., 1903, Compt. rend., 137, 1269
- Bertrand G., 1904, Ann. inst. Pasteur, 18, 116
- Bertrand G., 1907, Ann. inst. Pasteur, 21, 833
- Bertrand G., 1909, Compt. rend., 148, 297
- 10.1042/bj0292303 · doi:10.1042/bj0292303
- Bodansky M., 1919, J. Biol. Chem., 40, 127, 10.1016/S0021-9258(18)87271-4 · doi:10.1016/s0021-9258(18)87271-4
- Bokuchava M. A., 1948, Doklady Akad. Nauk U. S. S. R., 60, 409
- Bokuchava M. A., 1948, Biokhimiya, 13, 1
- Bondi C., 1951, Riv. Biol., 43, 331
- 10.3891/acta.chem.scand.01-0114 · doi:10.3891/acta.chem.scand.01-0114
- Bonnichsen R. K., 1947, Arch. Biochem., 12, 83
- 10.3891/acta.chem.scand.01-0685 · DOI
- 10.3109/13813453709145210 · doi:10.3109/13813453709145210
- Bourquelot E., 1896, Compt. rend., 123, 315
- Bourquelot E., 1904, Compt. rend., 138, 1432
- Brahn B., 1917, Biochem. Z., 79, 202
- Brandenburg K, 1900, Münch. med. Wochschr., 47, 183
- 10.3891/acta.chem.scand.07-0435 · doi:10.3891/acta.chem.scand.07-0435
- Brown O. H., 1904, Am. J. Physiol., 10, 335, 10.1152/ajplegacy.1904.10.7.378 · doi:10.1152/ajplegacy.1904.10.7.378
- Brocq‐Rousseu, 1907, Compt. rend., 145, 1297
- 10.1126/science.72.1872.505 · doi:10.1126/science.72.1872.505
- Burge W. E., 1916, Am. J. Physiol., 41, 153, 10.1152/ajplegacy.1916.41.2.153 · doi:10.1152/ajplegacy.1916.41.2.153
- Burnett T. C., 1918, Am. J. Physiol., 46, 43, 10.1152/ajplegacy.1918.46.2.63 · doi:10.1152/ajplegacy.1918.46.2.63
- 10.1002/path.1700260303 · doi:10.1002/path.1700260303
- Casolari, 1929, Biochim. e terap. sper., 16, 5203
- 10.1016/S0021-9258(18)44929-0 · doi:10.1016/s0021-9258(18)44929-0
- 10.3891/acta.chem.scand.01-0236 · DOI · Paper page
- 10.1038/161914a0 · DOI
- Chance B., 1949, Arch. Biochem., 21, 416
- Chance B., 1949, Arch. Biochem., 24, 389
- Chance B., 1949, Arch. Biochem., 24, 410
- Chance B., 1949, J. Biol. Chem., 179, 1341, 10.1016/S0021-9258(18)56799-5 · DOI
- 10.1042/bj0460387 · DOI · Paper page
- Chance B., 1950, Federation Proc., 9, 160
- Chance B., 1951, Enzymes and Enzyme Systems
- 10.1021/ja01160a041 · doi:10.1021/ja01160a041
- 10.1016/0003-9861(52)90470-0 · DOI · Paper page
- 10.1016/S0021-9258(18)55799-9 · DOI
- 10.1016/S0021-9258(18)55800-2 · DOI
- 10.1038/169215a0 · DOI · Paper page
- 10.1126/science.116.3008.202 · doi:10.1126/science.116.3008.202
- 10.1016/0003-9861(52)90194-X · DOI · Paper page
- 10.1042/bj0460402 · doi:10.1042/bj0460402
- 10.1039/jr9410000496 · doi:10.1039/jr9410000496
- Charmandarjan M. O., 1929, Biochem. Z., 207, 472
- Charrin, 1906, Compt. rend., 142, 595
- Chodat R., 1910, Abderhalden's Handbuch der biologischen Arbeitsmethoden, 3, 42
- Chodat R., 1925, Abderhalden's Handbuch der biologischen Arbeitsmethoden, 1, 319
- Clermont P., de, 1882, Compt. rend., 94, 1254
- Cotton S., 1901, Bull. soc. chim. France, 25, 255
- Crocker W., 1918, J. Agr. Research, 15, 137
- Cruess W. V., 1949, Food Technol., 3, 370
- Czyhlarz E., von, 1907, Hofmeisters Beiträge, 10, 358
- Deleano N. T., 1937, Bull. soc. chim. biol., 19, 808
- 10.1210/endo-38-3-137 · doi:10.1210/endo-38-3-137
- 10.3891/acta.chem.scand.05-0815 · doi:10.3891/acta.chem.scand.05-0815
- 10.3891/acta.chem.scand.06-1516 · doi:10.3891/acta.chem.scand.06-1516
- 10.1007/BF01358305 · doi:10.1007/bf01358305
- Dille R. S., 1948, J. Lab. Clin. Med., 33, 480
- 10.1042/bj0282061 · doi:10.1042/bj0282061
- 10.1016/S0021-9258(18)72638-0 · doi:10.1016/s0021-9258(18)72638-0
- 10.1126/science.89.2309.300 · doi:10.1126/science.89.2309.300
- Dounce A. L., 1950, Cancer Research, 10, 103
- 10.1021/ja01928a033 · doi:10.1021/ja01928a033
- 10.1093/oxfordjournals.aob.a090255 · doi:10.1093/oxfordjournals.aob.a090255
- Duncker F., 1911, Biochem. Z., 33, 253
- Dupouy R., 1903, Compt. rend. soc. biol., 55, 1000
- Dutcher R. A., 1918, J. Biol. Chem., 36, 63, 10.1016/S0021-9258(18)86420-1 · doi:10.1016/s0021-9258(18)86420-1
- Dutcher R. A., 1918, J. Biol. Chem., 36, 547, 10.1016/S0021-9258(18)86386-4 · doi:10.1016/s0021-9258(18)86386-4
- Ehrlich P., 1885, Das Sauerstoffbedürfnis des Organismus.
- 10.1042/bj0260010 · doi:10.1042/bj0260010
- 10.1042/bj0261281 · doi:10.1042/bj0261281
- 10.1515/bchm2.1909.59.5-6.327 · doi:10.1515/bchm2.1909.59.5-6.327
- Ephraim F., 1949, Inorganic Chemistry., 857
- 10.1042/bj0440035 · doi:10.1042/bj0440035
- Euler H., von, 1905, Z. physiol. Chem., 45, 420
- 10.1515/bchm2.1919.105.3-4.83 · doi:10.1515/bchm2.1919.105.3-4.83
- 10.1515/bchm2.1909.61.1.72 · doi:10.1515/bchm2.1909.61.1.72
- Euler H., von, 1920, Biochem. Z., 102, 124
- 10.1002/cber.19230560749 · doi:10.1002/cber.19230560749
- Euler H., von, 1927, Ann., 452, 158
- Euler H., von, 1927, Ann., 455, 1
- 10.1515/bchm2.1916.98.5-6.202 · doi:10.1515/bchm2.1916.98.5-6.202
- 10.1042/bj0020133 · doi:10.1042/bj0020133
- Eyster H. C., 1953, Ohio J. Sci., 53, 101
- Falk K. G., 1919, J. Biol. Chem., 38, 229, 10.1016/S0021-9258(18)87350-1 · doi:10.1016/s0021-9258(18)87350-1
- Farrell M. A., 1935, J. Bact., 29, 411, 10.1128/jb.29.4.411-435.1935 · doi:10.1128/jb.29.4.411-435.1935
- Favre W., 1911, Biochem. Z., 33, 32
- Feinstein R. N., 1949, J. Biol. Chem., 180, 1197, 10.1016/S0021-9258(19)51232-7 · doi:10.1016/s0021-9258(19)51232-7
- 10.1515/zpch-1911-0136 · doi:10.1515/zpch-1911-0136
- Fischl R., 1910, Wien. klin. Wochschr., 23, 1557
- 10.1038/icb.1948.32 · doi:10.1038/icb.1948.32
- Foulkes E. C., 1950, Enzymologia, 13, 302
- 10.1016/0003-9861(53)90419-6 · doi:10.1016/0003-9861(53)90419-6
- 10.1085/jgp.18.2.209 · doi:10.1085/jgp.18.2.209
- Friggeri A., 1938, Riv. Biol., 26, 5
- Fujita A., 1931, Biochem. Z., 232, 20
- Funk E., 1922, Biochem. Z., 128, 108
- 10.3891/acta.chem.scand.05-0781 · doi:10.3891/acta.chem.scand.05-0781
- 10.1038/160041a0 · DOI
- 10.1042/bj0440197 · doi:10.1042/bj0440197
- 10.1042/bj0540267 · doi:10.1042/bj0540267
- 10.1016/S0021-9258(18)71384-7 · DOI · Paper page
- Gjessing E. C., 1943, Arch. Biochem., 1, 1
- 10.1007/BF02153741 · doi:10.1007/bf02153741
- Goldblith S. A., 1950, J. Biol. Chem., 187, 705, 10.1016/S0021-9258(18)56216-5 · DOI
- Greenstein J. P., 1942, J. Natl. Cancer Inst., 2, 525
- Grüter R., 1911, Berl. klin. Wochschr., 48, 301
- 10.1021/ja01352a033 · DOI
- 10.1111/j.1748-1716.1913.tb00089.x · doi:10.1111/j.1748-1716.1913.tb00089.x
- 10.1042/bj0080217 · doi:10.1042/bj0080217
- 10.1016/S0021-9258(18)73400-5 · doi:10.1016/s0021-9258(18)73400-5
- 10.1002/j.1537-2197.1920.tb05576.x · doi:10.1002/j.1537-2197.1920.tb05576.x
- 10.1021/ja02216a025 · doi:10.1021/ja02216a025
- Heinicke A. J., 1933, J. Agr. Research, 46, 1137
- Hennichs S., 1924, Biochem. Z., 145, 286
- Hennichs S., 1926, Biochem. Z., 171, 314
- 10.1042/bj0430193 · DOI
- 10.1042/bj0430203 · DOI
- 10.1515/bchm2.1911.73.3-4.258 · doi:10.1515/bchm2.1911.73.3-4.258
- 10.1515/bchm2.1911.73.3-4.247 · doi:10.1515/bchm2.1911.73.3-4.247
- 10.1007/BF00898982 · doi:10.1007/bf00898982
- Hunger F. W. T., 1901, Ber. deut. botan. Ges., 19, 374, 10.1111/j.1438-8677.1901.tb05009.x · doi:10.1111/j.1438-8677.1901.tb05009.x
- 10.1111/j.1365-2621.1940.tb17222.x · doi:10.1111/j.1365-2621.1940.tb17222.x
- Huszék I, 1942, Biochem. Z., 312, 330
- Iglauer K., 1930, Biochem. Z., 223, 470
- Iscovesco H., 1905, Compt. rend. soc. biol., 58, 1054
- 10.1515/bchm2.1904.42.1-2.102 · doi:10.1515/bchm2.1904.42.1-2.102
- Itallie L., van, 1906, Compt. rend. soc. biol., 60, 148
- Jacobson J., 1892, Z. physiol. Chem., 16, 340
- Jacoby F., 1944, J. Physiol., 103, 22P
- Jacoby M., 1919, Biochem. Z., 92, 129
- Jamada K., 1908, Biochem. Z., 8, 61
- 10.1111/j.1469-8137.1943.tb04983.x · doi:10.1111/j.1469-8137.1943.tb04983.x
- Jayle M., 1938, Compt. rend. soc. biol., 128, 1074
- 10.1111/j.1365-2621.1947.tb16422.x · doi:10.1111/j.1365-2621.1947.tb16422.x
- Jolles A., 1903, Z. Biol., 45, 248
- Jorns A., 1908, Arch. Hyg., 67, 134
- Joslyn M. A., 1949, Advances in Enzymology, 613
- 10.1515/bchm2.1911.75.1-2.141 · doi:10.1515/bchm2.1911.75.1-2.141
- 10.1016/0095-8522(52)90004-4 · doi:10.1016/0095-8522(52)90004-4
- Kastle J. H., 1908, Am. Chem. J., 40, 251
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Metadata
- Authors
- Maehly, A. C.
- Venue
- Methods of Biochemical Analysis
- Publisher
- Wiley
- Published
- 1954-01
- Volume
- 1
- Pages
- 357-424
- ISSN
- 0076-6941 (ISSN-L)
- 1934-4325
- OpenAlex
- W1536654439
- Cited by
- 3,303
- References
- 0
- Type
- other
- Language
- en
- Open access
- closed
- Licence
- doi.wiley.com/10.1002/tdm_license_1.1 (tdm)
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