Enzimologia Diagnóstica
DOI:
https://doi.org/10.32635/2176-9745.RBC.1964v20n27.3742Keywords:
Pancreatic Neoplasms diagnosis, Enzymes/analysis, Enzyme Stability, 3-Hydroxysteroid DehydrogenasesAbstract
The A. makes a resumé of the presente status of'knowledge concerning the nature. origin and biological fate of enzymes. Methods of isolation of organ-speciíic enzymes and their potentialities in the diagnosis of tissue lesions are anlysed. Selective criteria of enzyme studies for diagnostic purposes are discussed. Serum lactic dehydrogenase and serum isocitric dehydrogenase, two of the so-called “metabolic” enzymes, are related in basic patterns of activity in several diaseases. Enzyme activities in myocardial infarction are discribed ande discussed, with particular emphasis on Hidroxibutiric dehydrogenase. An analysis of the compared activities of Glutamic oxaloacetic transaminase and Lactic de hydrogenase in pulmonary infarction is presented. Diagnostic and prognostic aspects of aldolase determinations in progressive muscular distrophy are discussed. A tabulation is made of enzyme activities in câncer diseases. The A. takes up the results of research of BODANSKY and cols. on Phosprohexose Isomerase and Aldolase in prognostic evaluation of mammary and prostatic câncer. A review is made on the importance of Acid and Alkaline phosphatase activities in primary and metastatic bone tumors and Ca. of the prostate. Particular mention is made of an outstanding paper by WETSTONE and cols. in which these auhors call attention to the low leveis of serum Cholinesterase in early diagnosis of cancer. The A. makes a critic review of enzyme activities in hepatitis, Laennec’s cirrhosis and the use of these tests in the differential diagnosis of intra-hepatic and post-hepatic jaundice. The last section of the paper deals with enzyme studies in hereditary diseases caused by primary disturbances of enzyme control. The A. calls attention to the recently divised “Dibucaine Number test to detect congenital abnormalities of Cholinesterase activity. Since a clear-cut clinicai picure does not occur in these patients, their detection is extremely important. When exposed to Cholinesterase inhibitors they go into prolonged respiratory arrest which may be fatal. The A. advocates the inclusion of the “Dibucaine Number” test as a routine procedure on admission of I.N.C. patients in order to avoid the catastrophic results of some of the often-used Cholinesterase inhibitors.
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References
AGREN, G., e LAGERLOF, H. O., Acta Med. Scand., 32, 359, 1937. DOI: https://doi.org/10.1111/j.0954-6820.1937.tb09956.x
AGRESS, C. M., Evaluation of the Transaminase Test., Am. J. Cardiol., 3: 74-93, 1959. DOI: https://doi.org/10.1016/0002-9149(59)90398-4
BODANSKY, O., Enzymes in Tumor Growth, in “Enzymes in Health and Disease”, Charles C. Thomas — 1960 Ed.
BODANSKY, O., Diagnostic Applications of Enzymes in Medicine. Am. J. Med. '861-874, N.° 6, Dec. 1959. DOI: https://doi.org/10.1016/0002-9343(59)90172-X
BROWN, M. E., New England L Med. 260, 331, 1959. DOI: https://doi.org/10.1056/NEJM195902122600707
BURTON, P. EVANS, D. G., HARPER, A. A., etc., Gut., 1, 111 e 1, 125. DOI: https://doi.org/10.1136/gut.1.2.111
COOKE, K. B., e ZILVA, J. F., J. Clin. Path., 14, 500, 1961. DOI: https://doi.org/10.1136/jcp.14.5.500
DIXON, T. F. e PURDOM, M., J. Clin. Path., 7, 341, 1954. DOI: https://doi.org/10.1136/jcp.7.4.341
DREYFUS, J. C., SCHAPIRA, G., e SCHAPIRA, F., Ann. N. Y. Acad. Sci. 75, 235, 1958. DOI: https://doi.org/10.1111/j.1749-6632.1958.tb36870.x
DUNCAN, P. R., HARPER, A. A., HOWAT, H. T., OLEESKY, S. e VARLEY, H., J. Physiol., 111, 63 P., 1950.
ELLIOTT, B. A., e WILKINSON, J. H., Lancet, i, 698, 1961. DOI: https://doi.org/10.1016/S0140-6736(61)91724-X
EISHMAN, W. H., BONNER, C. D., HOMBURGER, E., New England J. Med., 255, 925, 1956. DOI: https://doi.org/10.1056/NEJM195611152552001
GUTMAN, A. B., Amer. J. Med. 27, 875, 1959. DOI: https://doi.org/10.1016/0002-9343(59)90173-1
HARRIS, H., WHITTAKER, M., LEHMANN, H., e SILK, E., Acta genet., 10, 1, 1960. DOI: https://doi.org/10.1159/000151112
HUNT, A. H., e LEHMAN, H., J. Clin. Path., 12, 583, 1959.
KALOW, W., Biochemistry of Human Genetics. Giba Found. Symp. Ed. Churchill — London — pag. 39.
KAUEMAN, K., Ann. intern. Med., 41, 553, 1954. DOI: https://doi.org/10.7326/0003-4819-41-3-553
KEIDING, N. R., Scand. J. Clin. Lab. Invest. 11, 106, 1959. DOI: https://doi.org/10.3109/00365515909060415
LA DUE, J. S., KARMEN, A., WRÓBLEWSKI, F. Science, 120, 497, 1954. DOI: https://doi.org/10.1126/science.120.3117.497
LA MOTTA, R. V., WILLIAMS, H. M., WETSTONE, H. J., Gastroenterology, 33, 50, 1957. DOI: https://doi.org/10.1016/S0016-5085(19)35788-9
LATNER, A., SMITH, A. J., Lancet. ii, 195, 1958.
MOSS, D. W., CAMPBELL, D. M. ANAGNOSTOU-KAKARAS, E., KING, E. J., Biochem. J., 81, 441, 1961. DOI: https://doi.org/10.1042/bj0810441
MOSS, D. W., CAMPBELL, D. M., ETC., Pure and Appl. Chem. 3, 397, 1961. DOI: https://doi.org/10.1351/pac196103030397
NARDI, G. L., J. Lab. Clin. Med., 52, 66, 1958.
NISSELBAUM, J. S., BODANSKY, O., J. Biol. Chem., 234, 3.276, 1959. DOI: https://doi.org/10.1016/S0021-9258(18)69664-4
NISSELBAUM, J. S., BODANSKY, O., J. Biol. Chem., 236, 401, 1961. DOI: https://doi.org/10.1016/S0021-9258(18)64375-3
OKUMURA, M., e SPELLBERG, M. A., Gastroenterology, 39, 305, 1960. DOI: https://doi.org/10.1016/S0016-5085(19)35265-5
PLAGEMANN, P. P. W., GREGORY, K. F., e WRÓBLEWSKI, F. J., Biol. Chem. 235, 2.282, 1960. DOI: https://doi.org/10.1016/S0021-9258(18)64613-7
POPPER, H., e SCHAFFNER, F., in “Liver, Structure an Fruction”, Ed. McGraw Hill. N. York, 1957.
REICHARD, H., J. Lab. Clin. Med., 57, 78, 1961.
REIS, J. L., Bull. Soc. Chem. Biol. 16, 385, 1934.
ROBERTS, W. M., Brit. Med. J., i, 734, 1933. DOI: https://doi.org/10.1136/bmj.1.3773.734
ROSALKI, S. B., e WILKINSON J. H., Nature, 188, 1.110, 1960. DOI: https://doi.org/10.1038/188110a0
ROSEMBERG, 1. N., J. Clin. Invest. 38, 630, 1959. DOI: https://doi.org/10.1172/JCI103841
SIBLEY, J. A., LEHNINGER, A. L., J. Nat. Câncer Inst. 9, 303, 1949.
SILVERMAN, L, LIVINGSTON, S. F., Cancer, 13, 921, 1960. DOI: https://doi.org/10.1002/1097-0142(196009/10)13:5<921::AID-CNCR2820130510>3.0.CO;2-1
STRANDJORD, P. E., THOMAS, K. E., e WHITE, L. P., J. Clin. Invset. 38, 2.111, 1960.
SUN, D. C. H., e SHAY, H., Gastroenterology, 38, 570, 1960. DOI: https://doi.org/10.1016/S0016-5085(60)80030-3
VESEL, E. S., e BERN, A. G., Ann. N. Y. Acad. Sei., 75, 826, 1958.
VORHAUS, L. J. e KARK, R. M., Amer. J. Med., 14, 707, 1953. DOI: https://doi.org/10.1016/0002-9343(53)90390-8
YOUNG, I. L, Ann. N. Y. Acad. Sci., 75, 357, 1958. DOI: https://doi.org/10.1111/j.1749-6632.1958.tb36883.x
WETSTONE, H. J., LA MOTTA, R. V., BELLUCCI, A., TENNANT, R., e WHITE, B. B., Ann. Intern. Med.., 52, 102, 1960. DOI: https://doi.org/10.7326/0003-4819-52-1-102
WHITE. L. P., Advances in die Diagnostic Use of Enzymes — in “Enzymes in Health and Disease”. Charles C. Thomas — 1960.
WILKINSON, J. H., An Introduction to Diagnostic Enzymology — Ed. Arnold. 1962.
WRÓBLEWSKI, F., e LA DUE, J. S., Proc. Soc. exp. Biol. N. Y. 90, 210, 1955. DOI: https://doi.org/10.3181/00379727-90-21985
MACLAGAN, N. F., Differential Diagnosis of Jaundice, Brit. Med. Jour. 2, 197, 1947. DOI: https://doi.org/10.1136/bmj.2.4518.197