Skip to main content

Influence of black gram(Vigna mungo) trypsin inhibitory fraction on the hepatic protein catabolism in male albino mice

Research in Experimental Medicine volume 184, pages 85–90 (1984)Cite this article

Summary

The effect of black gram and black gram trypsin inhibitor on the protein catabolism of male albino mice has been investigated. Group I was given autoclaved black gram (control), Group II raw black gram and Group III the autoclaved black gram incorporated with 1% black gram trypsin inhibitor. Blood as well as urinary urea and creatinine were found to be elevated in Groups II and III. Increased levels of arginase, ornithine transcarbamylase and transaminases were noted in Groups II and III. The results suggested an enhanced catabolism of proteins evoked by the native black gram trypsin inhibitor.

This is a preview of subscription content, access via your institution.

References

  1. Das TK, Waterlow JC (1974) The rate of adaptation of urea cycle enzymes, aminotransferases, and glutamic dehydrogenase to changes in dietary protein intake. Br J Nutr 32:353–373

    PubMed  Google Scholar 

  2. Hayase K, Yokogoshi H, Yoshida A (1980) Effect of dietary proteins and amino acid deficiencies on urinary excretion of nitrogen and the urea synthesizing system in rats. J Nutr 110:1327–1337

    PubMed  Google Scholar 

  3. Kamalakannan V, Motlag DB (1982) Influence of dietary black gram (Vigna mungo) trypsin inhibitor on the growth rate and nitrogen absorption in male albino mice. Nutr Rep Int 25:113–125

    Google Scholar 

  4. Cenarruzabeitia MN, Santidrian S, Bello J, Larralde J (1979) Effect of raw field bean(Vicia faba) on amino acid degrading enzymes in rats and chicks. Nutr Metab 23:203–210

    PubMed  Google Scholar 

  5. Sathyamoorthy V, Kamalakannan V, Motlag DB (1981) Influence of dietary raw green gram (Phaseolus aureus, Roxb) and green gram trypsin inhibitors on the activity of certain protein metabolism enzymes in rats. Ann Nutr Metab 25:334–340

    PubMed  Google Scholar 

  6. Kamalakannan V, Sathyamoorthy V, Motlag DB (1981) Studies on black gram(Vigna mungo) trypsin inhibitor. J Sci Food Agric 32:1172–1176

    PubMed  Google Scholar 

  7. Natelson S (1961) Urea with diacetyl monoxime. In: Natelson S (ed) Microtechniques of clinical chemistry. Thomas, Springfield, Ill, pp 434–437

    Google Scholar 

  8. Bonsnes RW, Taussky HH (1945) On the colorimetric determination of creatinine by the Jaffe reaction. J Biol Chem 158:581–591

    Google Scholar 

  9. Varley H (1967) Determination of creatinine. In: Varley H (ed) Practical clinical biochemistry. ELBS, New York, pp 199–200

    Google Scholar 

  10. Schimke RT (1962) Adaptive characteristics of urea cycle enzymes in the rat. J Biol Chem 237:459–468

    PubMed  Google Scholar 

  11. Ohshita M, Takeda H, Kamiyama Y, Ozawa K, Honjo I (1976) A direct method for the estimation of ornithine carbamoyl transferase activity in serum. Clin Chem Acta 67:145–152

    Google Scholar 

  12. Archibald RM (1944) Determination of citrulline and allantoin and demonstration of citrulline in blood plasma. J Biol Chem 156:121–142

    Google Scholar 

  13. Reitman S, Frankel S (1957) A colorimetric method for the determination of serum glutamic oxaloacetic and glutamic pyruvic transaminases. Am J Clin Pathol 28:56–63

    PubMed  Google Scholar 

  14. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275

    PubMed  Google Scholar 

  15. Bernstein J, Weatherall M (1952) In: Statistics for medical and other biological students. Williams and Wilkins, Baltimore

    Google Scholar 

  16. Kean EA (1967) The relationship between nutritive value of dietary protein and activity of liver arginase and kidney transamidinase enzymes. Br J Nutr 21:29–36

    PubMed  Google Scholar 

  17. Sathyamoorthy V, Kamalakannan V, Motlag DB (1982) Effect of dietary green gram trypsin inhibitor and raw green gram meal (Phaseolus aureus, Roxb) on the pancreatic activity in rats. Res Exp Med (Berl) 180:169–178

    Google Scholar 

  18. Hagihira H, Lin ECC, Samiy AH, Wilson TH (1961) Active transport of lysine, ornithine, arginine and cystine by the intestine. Biochem Biophys Res Commun 4:478–481

    PubMed  Google Scholar 

  19. Robinson JWL (1966) In: Frotscher KGH (ed) Certain aspects of intestinal amino acid absorption. Odenwald, Darmstadt, pp 1

    Google Scholar 

  20. Munck BG (1965) Amino acid transport by the small intestine of the rat. The effect of amino acid preloading on the trans-intestinal amino acid transport by the everted sac preparation. Biochem Biophys Acta 109:142–150

    PubMed  Google Scholar 

  21. Munck BG, Schultz SG (1969) Lysine transport across isolated rabbit ileum. J Gen Physiol 53:157–182

    PubMed  Google Scholar 

  22. Kamalakannan V, Sathyamoorthy V, Motlag DB (1984) Purification, characterisation and kinetics of a trypsin inhibitor from black gram(Vigna mungo). J Sci Food Agric 35:199–206

    Google Scholar 

Download references

Author information

Affiliations

  1. Dept. of Biochemistry, University of Madras, Guindy Campus, 600 025, Madras, India

    V. Kamalakannan, A. V. Sathyamoorthy & D. B. Motlag

Authors
  1. V. Kamalakannan
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. A. V. Sathyamoorthy
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. D. B. Motlag
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Kamalakannan, V., Sathyamoorthy, A.V. & Motlag, D.B. Influence of black gram(Vigna mungo) trypsin inhibitory fraction on the hepatic protein catabolism in male albino mice. Res. Exp. Med. 184, 85–90 (1984). https://doi.org/10.1007/BF01852355

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01852355

Key words

  • Black gram trypsin inhibitor
  • Protein catabolism