[Action of proteinase inhibitors. 4. Effect of short-term application of chymostatin on nitrogen metabolism in the digestive tract and protein metabolism in tissue].

Chymostatin is an effective inhibitor of intracellular proteinases in vitro. In the present experiment male rats were injected intraperitonealy during a 3 days period twice daily with a solution containing 0,9 mg Chymostatin per 100 g live weight. Reference animals received a control injection containing the same solvents but no chymostatin. During this period a daily nitrogen balance was made and metabolic faecal nitrogen and true digestibility of nitrogen were estimated using 15N-labelled animals. Furthermore, apparent biological half lives of proteins in liver and intestinal tissues were determined following the decay curves for radioactivity in proteins 48 hours after injection of L-[5-3H]-arginine und L-[guanido-14C]-arginine. The fractional rate of protein synthesis in tissues was measured by a 6 hours continuous infusion technique with L-[U-14C]-tyrosine and L-[U-14C]-leucine. Among the parameters estimated only the apparent biological half lives of proteins in liver and intestinal tissues were influenced by chymostatin. However, the prolonged half lives seemed to be rather an effect of an increased reutilisation of amino acids resulting from the intracellular protein breakdown than a decreased rate of protein degradation. The in vivo effect of the proteinase inhibitor was by far inferior compared with the action in vitro. Factors like distribution, degradation and excretion of the inhibitor could be responsible for the moderate in vivo action of chymostatin.

[1]  H. Bergner,et al.  [Methodologic studies on endogenous N excretion in feces using N15-labeled compounds in test rats]. , 1983, Archiv fur Tierernahrung.

[2]  R. Beynon,et al.  Tissue and subcellular distribution of enzymes inactivating leupeptin , 1983, Bioscience reports.

[3]  M. Hernández,et al.  [A new method for testing the quality of food proteins for maintenance metabolism. 4. Testing of isolated proteins as well as various protein sources of plant and animal origin]. , 1981, Archiv fur Tierernahrung.

[4]  M. Hernández,et al.  [A new method for testing the quality of food proteins for maintenance metabolism. 3. Methodological studies of 15N-labeled adult rats]. , 1981, Archiv fur Tierernahrung.

[5]  O. Simon,et al.  Effect of thyroid hormones on the in vivo protein synthesis in rats. , 1981, Archiv fur Tierernahrung.

[6]  E. Wolf,et al.  Untersuchungen zur Charakterisierung der Radioaktivitätsverteilung im Organismus bei konstanter intravenöser Infusion von Traceraminosäuren bei Ratten und zur Berechnung der Gewebeproteinsyntheserate , 1978 .

[7]  H. Bergner,et al.  [New method of checking the quality of food proteins required for maintenance. 2. 15N excretion in feces of test rats labelled with 15N after feeding with different protein sources]. , 1978, Archiv fur Tierernahrung.

[8]  K. Krawielitzki,et al.  Tracerversuche an Ratten mit 15N-markiertem Weizen zur Bestimmung des endogenen und exogenen fäkalen N-Anteils , 1978 .

[9]  H. Kirschke,et al.  PROTEIN CATABOLISM IN RAT LIVER CELLS , 1978 .

[10]  P. Bohley,et al.  [Mode of action of proteinase inhibitors in rats. 2. Effect of leupeptin on N-balance and biological half-life in ad lib feeding]. , 1977, Archiv fur Tierernahrung.

[11]  K. Krawielitzki,et al.  Versuche zur Bestimmung des endogenen und exogenen fäkalen N-Anteiles monogastrischer Tierarten , 1977 .

[12]  H. Bergner,et al.  Untersuchungen zur Wirkung von Proteinaseinhibitoren bei Ratten , 1976 .

[13]  D. J. Millward,et al.  The diurnal response of muscle and liver protein synthesis in vivo in meal-fed rats. , 1973, The Biochemical journal.

[14]  H. Umezawa Enzyme inhibitors of microbial origin , 1972 .

[15]  H. Lehmann Ratten-Stoffwechselkäfig zur quantitativen Kotund Harntrennung bei N-Bilanzuntersuchungen , 1968 .

[16]  O. H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.