Abstract
It has been shown that lignosulphonic acids have an inhibitory effect on various animal and microbial proteinases. The activity of 0.005 mg swine trypsin, 0.007 mg bovine a-chymotrypsin and the proteinase activity in 0.004 ml of jejunum content from pig is inhibited 70–75 % by 0.25–0.30 ml of a solution containing 250 diffusion units of peptide-precipitating lignosulphonic acids per 50 µl.
The inhibitory effect is discussed in relation to the use of animal foodstuffs containing lignosulphonic acids, and in relation to biochemical reactions taking place in ecosystems in which lignosulphonic acids comprise an important part.
Keywords: lignosulphonic acids, proteinase inhibition, animal proteinases, microbial proteinases
Sammendrag
Det er vist at ligninsulfonsyrer har hemmende virkning på forskjellige animalske og mikrobielle proteinaser. Aktiviteten av 0,005 mg svinetrypsin, 0,007 mg a-chymotrypsin fra storfe og proteinaseaktiviteten i 0,004 ml jejunuminnhold fra gris kan inhiberes 70–75 % med 0,25–0,30 ml av en løsning som inneholder 250 diffusjonsenheter peptidpresipiterende ligninsulfonsyrer per 50 µl.
En har diskutert den hemmende virkningen i forhold til bruken av visse forstoffer som inneholder ligninsulfonsyrer og i forhold til biokjemiske reaksjoner som finner sted i økosystemer hvor ligninsulfonsyrer utgjør en viktig del.
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References
- Fossum, K.: Proteolytic enzymes and biological inhibitors I. Comparison between the Kunitz method and the agar gel casein precipitating reaction for determination of the activity of some commercial proteolytic enzymes and inhibitors. Acta path. microbiol. scand. 78B, 1970a, 350–362. [PubMed]
- Fossum, K.: Proteolytic enzymes and biological inhibitors IV. Bacterial proteinase inhibitors and their effect upon enzymes of various origin. Acta path. microbiol. scand. 78B, 1970b, 755–759. [PubMed]
- Hildrum K I, Næss B. Gel filtration of lignosulphonic acids and peptide-precipitating abilities of the separated fractions. Acta vet. scand. 1972;13:293–304. doi: 10.1186/BF03547047. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jantzen, L.: Lignoprotein, animal feed. Aktieselskapet Christiania Portland Cementfabrik. Brit. 1.092.628 (Cl.C.07g), Nov. 29, 1967, Appl. Nov. 26, 1964.
- Kunitz, M.: Crystalline soybean trypsin inhibitor II. General properties. J. gen. Physiol. 30, 1947, 291–310. [DOI] [PMC free article] [PubMed]
- Melmed R N, Bouchier I A D. A further physiological role of naturally occurring trypsin inhibitors: The evidence for a trophic stimulant of the pancreatic ancinar cell. Gut. 1969;10:973–979. doi: 10.1136/gut.10.12.973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Næss, B.: Peptide-lignosulphonic acid precipitation zones in agar gel. A direct micro quantitative procedure for the determination of peptide-precipitating lignosulphonic acids in aqueous solution. Acta vet. scand. 1971a, 12, 583–591. [DOI] [PMC free article] [PubMed]
- Næss, B.: Mikrobielle omsetninger i avfallsvann fra treforedlingsprosesser i ressursmessig og økologisk sammenheng. (Microbial activity in waste waters from chemical wood pulp processes, in relation to ecology and natural resources). Norsk vet.-T. 1971b, 10, 501–506.
- Næss, B.: The effect of microbial and animal proteinases on peptideand protein-lignosulphonic acid complexes in agar gel. Acta vet. scand. 1971c, 12, 592–600. [DOI] [PMC free article] [PubMed]
- Næss, B.: The effect of proteinase-digested peptide-lignosulphonic acid complexes, dipeptides and amino acids on the formation of peptide-lignosulphonic acid precipitates. Acta agric. scand. 21, 1971d, 199–207.
- Næss B, Westbye O, Hildrum K I, Nafsiad I. The effects of peptide-precipitating lignosulphonic acids on the proteolytic activity of pepsin in vitro and on the response of pigs to an ulcer inducing diet. Acta vet. scand. 1973;14:44–56. doi: 10.1186/BF03547409. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sandvik, O.: Studies on casein precipitating enzymes of aerobic and facultatively anaerobic bacteria. Thesis. Veterinary College of Norway, Oslo 1962.