Abstract
Colostral trypsin-inhibitor capacity was monitored during the first two weeks from parturition. The colostrum of the mare, sow, cow and ewe showed high antitrypsin activity at parturition, decreasing to about one hundredth during the first week. Canine milk remained on a relatively high antitrypsin level, and human milk was poor in antitrypsin from childbirth. The antitrypsin content seems to parallel the known changes in the colostral immunoglobulin levels of different species. The role of antitrypsin in protection of immunoglobulins from proteolytic damage during passive transfer of immunity to the newborn is obvious.
Keywords: colostrum, trypsin inhibitor, protease inhibitors, colostral albumin
Sammanfattning
Kolostrum av sto, sugga, ko och tacka innehöll en hög trypsinhämmande kapacitet efter förlossningen. Aktiviteten sjönk till cirka en hundrade del under första veckan. Kolostrum från tikar innehöll en längre tid en högre antitrypsinaktivitet, men däremot är aktiviteten i modersmjölken låg redan från början.
Antitrypsinaktiviteten tycks följa immunoglobulinmängden. Antitrypsinet kan tänkas skydda immunoglobulinerna från proteolys under den passiva intestinala transporten av immunoglobulinerna till det nyfödda djuret.
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References
- Butler, J. E.: Immunoglobulins of the mammary secretions. In Lactation, vol. III. Larson, B. L. & Smith, V. L., eds. Acad. Press 1974, p. 217–255.
- Carlsson L., Karlsson B. Gel diffusion methods for determination of protease and protease-inhibiting activities. Experientia. 1972;28:990–991. doi: 10.1007/BF01924992. [DOI] [PubMed] [Google Scholar]
- Carlsson L. C. T., Bergelin I. S. S., Karlsson B. W. Trypsin inhibition in urine of developing neonatal pigs and in sow’s colostrum. Enzyme. 1974;18:176–188. doi: 10.1159/000459424. [DOI] [PubMed] [Google Scholar]
- Cechova, D.: Trypsin inhibitor from cow colostrum. In Methods in Enzymology. Vol. XLV, Proteolytic Enzymes, Part B, Laszlo Lorand, ed. Acad. Press 1976, p. 806–813. [DOI] [PubMed]
- Chamberlain, A. G. & G. C. Perry: Effect of trypsin inhibitor isolated from sow’s colostrum on the absorption of γ-globulin by piglets. Nature (Lond.) 1965, 207, 429. [DOI] [PubMed]
- Fossum K. Proteolytic enzymes and biological inhibitors. Acta path. microbiol. scand. B. 1970;78:350–362. [PubMed] [Google Scholar]
- Jensen P. T. Trypsin inhibitor and immunoglobulins in porcine colostrum. Acta vet. scand. 1978;19:475–477. doi: 10.1186/BF03547620. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Laskowski M., Laskowski M. Crystalline trypsin inhibitor from colostrum. J. biol. Chem. 1951;190:563–573. [PubMed] [Google Scholar]
- Laskowski M., Kassier B., Hagesty G. A crystalline trypsin inhibitor from swine colostrum. Biochim. biophys. Acta (Amst.) 1957;24:300–305. doi: 10.1016/0006-3002(57)90198-1. [DOI] [PubMed] [Google Scholar]
- Mancini G., Carbonara A. O., Heremans J. F. Immunochemical quantitation of antigens by single radial immunodiffusion. Immunoehemistry. 1965;2:235–254. doi: 10.1016/0019-2791(65)90004-2. [DOI] [PubMed] [Google Scholar]
- Pineiro A., Ortega F., Uriel J. Trypsin inhibitor from cow colostrum. Isolation electrophoretic characterization and immunologic properties. Biochim. biophys. Acta (Amst.) 1975;379:201–206. doi: 10.1016/0005-2795(75)90023-9. [DOI] [PubMed] [Google Scholar]
- Sandholm M., Smith R. R., Shih J. C. H., Scott M. L. Determination of antitrypsin activity on agar plates: Relationship between antitrypsin and biological value of soybean for trout. J. Nutr. 1976;106:761–766. doi: 10.1093/jn/106.6.761. [DOI] [PubMed] [Google Scholar]
- Sandvik, O.: Studies on casein precipitating enzymes of aerobic and facultatively anaerobic bacteria. Veterinary College of Norway, Thesis 1962.