Advertisement

The Japanese journal of surgery

, Volume 20, Issue 4, pp 392–405 | Cite as

The significance of serum mitochondrial aspartate aminotransferase activity in obstructive jaundice: Experimental and clinical studies

  • Eishin Sada
  • Seiki Tashiro
  • Yoshimasa Morino
Original Articles

Abstract

The serum level of mitochondrial aspartate aminotransferase was determined in experimental and clinical obstructive jaundice, using an immunoabsorbance method which allowed the differential determination of cytosolic and mitochondrial isozymes in the serum. In experimental obstructive jaundice using dogs, the serum mitochondrial aspartate aminotransferase value rapidly decreased to normal after biliary decompression following a period of biliary obstruction of within 3 weeks. On the other hand, when the period of jaundice was prolonged for 5 weeks, the activity of the enzyme after biliary drainage still continued to show high values, being 14.2±1.8 Karmen units at 4 weeks following biliary decompression. Determination of aspartate aminotransferase activity in tissue from such organs as the liver, heart, kidney, skeletal muscle and brain, as well as serum samples with drawn from local veins, confirmed that high serum values of the enzyme in experimental obstructive jaundice were mostly attributable to hepatic impairment induced by biliary obstruction not by secondarily damaged tissues of other organs. Mitochondrial aspartate aminotransferase proved to be a more useful marker than other routine tests in icteric dogs. In 13 clinical patients with obstructive jaundice, decreasing rates of serum mitochondrial aspartate aminotransferase on the 7th and 14th postoperative days could be applied to evaluate the viability of the icteric liver. The decreasing rates were more advantageous than the preoperative activity itself in predicting the postoperative function of the liver. Thus, mitochondrial aspartate aminotransferase appears to serve as a useful marker for assessing the liver function in obstructive jaundice.

Key Words

biliary decompression liver function test mitochondrial aspartate aminotransferase 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Moody FG, Rikkers LF, Aldrete JS. Estimation of the functional reserve of human liver. Ann Surg 1974; 180: 592–598.PubMedGoogle Scholar
  2. 2.
    Ozawa K, Yamaoka Y, Kitamura O, Nambu H, Kamiyama Y, Takeda H, Takasan H, Honjo I. Clinical application of cytochrome a (+a3) assay of mitochondria from liver specimens: An aid in determining metabolic tolerance of liver remnant for hepatic resection. Ann Surg 1974; 180: 868–876.PubMedCrossRefGoogle Scholar
  3. 3.
    Fleisher GA, Potter CS, Wakim KG. Separation of 2 glutamic-oxalacetic transaminases by paper electrophoresis. Proc Soc Exp Biol Med 1960; 103: 229–231.PubMedGoogle Scholar
  4. 4.
    Boyde TRC, Latner AL. Starch-gel electrophoresis of transaminases in human tissue extracts and sera. Biochem J 1962; 82: 51.Google Scholar
  5. 5.
    Awapara J, Seale B. Distribution of transaminases in rat organs. J Biol Chem 1952; 194: 492–502.Google Scholar
  6. 6.
    Björkerud S, Björntorp P, Scherstén J. Lysosomal enzyme activity in human liver in relation to the age of the patient and in cases with obstructive jaundice. Scand J Clin Lab Invest 1967; 20: 224–230.Google Scholar
  7. 7.
    Ishida A. Solubilization and partial purification of cytochrome P-450 from hepatic microsomes of phenobarbital treated rat. Kumamoto Med J 1976; 29: 134–145.PubMedGoogle Scholar
  8. 8.
    Hogeboom GH, Schneider WC, Pallade GE. Cytochemical studies of mammalian tissues. 1. Isolation of intact mitochondria from rat liver; some biochemical properties of mitochondria and submicroscopic particulate material. J Biol Chem 1948; 172: 619–635.PubMedGoogle Scholar
  9. 9.
    Loiselle JM, Denstedt OF. Biochemical changes during acute physiological failure in the rat. Can J Biochem 1964; 42: 21–34.CrossRefGoogle Scholar
  10. 10.
    Gornall AG, Bardawill CJ, David MM. Determination of serum proteins by means of the biuret reaction. J Biol Chem 1949; 177: 751–766.PubMedGoogle Scholar
  11. 11.
    Ozawa K, Takasan H, Kitamura O, Mizukami T, Kamano T, Takeda H, Ohsawa T, Murata T, Honjo I. Effect of ligation of portal vein on liver mitochondrial metabolism. J Biochem 1971; 70: 755–764.PubMedGoogle Scholar
  12. 12.
    Kodama M, Tanaka T, Kodama O, Harada M, Takeuchi H, Itoh N. Indications and problems for gastroenterological surgery in patients with hepatic dysfunction-special reference to the evaluation of routine liver function tests. Nippon Shokaki Geka Gakkai Zasshi (Jpn J Gastroenterol Surg) 1982 15: 680–695. (in Japanese)Google Scholar
  13. 13.
    Tashiro S, Ogata K, Yamasaki K, Hayashida N, Sada E, Murata E, Hiraoka T. Surgery in patients with hepatic dysfunction. Nippon shokaki Geka Gakkai Zasshi (Jpn J Gastroenterol Surg) 1982; 15: 686–692. (in Japanese)Google Scholar
  14. 14.
    Wada H, Teranishi H Kagamiyama H, Ohyanagi H, Shirakawa H, Mitsuno T, Fuse K, Sawada Y. A simple immunological method for differential determination of serum glutamic-oxaloacetic transaminase isoenzymes. (1) Using anti-human-GOT antibody. Med J Osaka Univ 1978; 29: 181–190.PubMedGoogle Scholar
  15. 15.
    Teranishi H, Wada H, Sawada Y. A simple immunological method for differential determination of serum glutamic-oxaloacetic transaminase isoenzymes. (II) Using anti-pig-GOT antibody. Med J Osaka Univ 1978; 29: 191–198.PubMedGoogle Scholar
  16. 16.
    Karmen A, Wróblewski F, LaDue JS. Transaminase activity in human blood. J Clin Invest 1955; 34: 126–131.PubMedCrossRefGoogle Scholar
  17. 17.
    Malloy HT, Evelyn KA. The determination of bilirubin with the photoelectric colorimeter. J Biol Chem 1937; 119: 481–490.Google Scholar
  18. 18.
    Doumas BT, Watson W ARD, Giggs HG. Albumin standards and the measurement of serum albumin with bromcresol green. Clin Chim Acta 1971; 31: 87–96.PubMedCrossRefGoogle Scholar
  19. 19.
    Person DA, Judge RD. Effect of operation on serum transaminase levels. Arch Surg 1958; 77: 892–897.Google Scholar
  20. 20.
    Wróblewski F, LaDue JS. Serum glutamic oxalacetic transaminase activity as an index of liver cell injury: A preliminary report. Ann Intern Med 1955; 43: 345–359.PubMedGoogle Scholar
  21. 21.
    Boyd JW. The intracellular distribution, latency and electrophoretic mobility of L-glutamate-oxaloacetate transaminase from rat liver. Biochem J 1961; 81: 434–441.PubMedGoogle Scholar
  22. 22.
    Narpas B, Vassault A, Guillou AL, Lesgourgues B, Ferry N, Lacour B, Berthelot P. Serum activity of mitochondrial aspartate aminotransferase: A sensitive marker of alcoholism with or without alcoholic hepatitis. Hepatology 1984; 4: 893–896.CrossRefGoogle Scholar
  23. 23.
    Ozawa K, Ida T, Yamada T, Yamaoka Y, Takasan H, Honjo I. Oral glucose tolerance in patients with jaundice. Surg Gynecol Obstet 1975; 140: 582–588.PubMedGoogle Scholar
  24. 24.
    Sato N, Koyama M, Hayashi N, Shichiri M, Kamada T, Abe H. A relationship between serum m-GOT and liver respiratory activity. Kanzo (Acta Hepatologica Japonica) 1982; 23: 361–363. (in Japanese with English Abst.)Google Scholar

Copyright information

© The Japan Surgical Society 1990

Authors and Affiliations

  • Eishin Sada
    • 2
  • Seiki Tashiro
    • 2
  • Yoshimasa Morino
    • 1
  1. 1.The Second Department of BiochemistryKumamoto University Medical SchoolKumamotoJapan
  2. 2.The First Department of SurgeryKumamoto University Medical SchoolKumamotoJapan

Personalised recommendations