In vitro interaction of porcine serum and colostrum protease inhibitors with pancreatic trypsin, chymotrypsin and elastase
(1982) In Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 705(3). p.357-365- Abstract
The partition of 125I-labelled pancreatic trypsin, chymotrypsin and elastase between the inhibitors, α2-macroglobulin f and s, α1-protease inhibitor, α2-antitrypsin, inter-α-trypsin inhibitor and the specific sow colostrum protease inhibitor, was studied in vitro by gradually increasing the concentration of these proteases in blood serum from adult and newborn pigs. As revealed by immunoelectrophoresis in combination with autoradíography, dífferences were noted in the abilities of the various protease inhibitors to interact with and to form complexes with the three proteases, resulting in changes in location, height and numbers of precipitates. Among the serum inhibitors,... (More)
The partition of 125I-labelled pancreatic trypsin, chymotrypsin and elastase between the inhibitors, α2-macroglobulin f and s, α1-protease inhibitor, α2-antitrypsin, inter-α-trypsin inhibitor and the specific sow colostrum protease inhibitor, was studied in vitro by gradually increasing the concentration of these proteases in blood serum from adult and newborn pigs. As revealed by immunoelectrophoresis in combination with autoradíography, dífferences were noted in the abilities of the various protease inhibitors to interact with and to form complexes with the three proteases, resulting in changes in location, height and numbers of precipitates. Among the serum inhibitors, α2-macroglobulins showed the highest relative affinity to all three proteases, while α1-protease inhibitor showed a high relative affinity only for chymotrypsin. Serum α2-antitrypsin complexed only with trypsin, with a low relative affinity, α2-Antitrypsin also interacted with chymotrypsin and elastase, but without forming complexes. When complexes of sow colostrum protease inhibitor and trypsin were added to the serum from neonatal pigs, these complexes remained stable. The results obtained from these in vitro studies, indicating differences in the relative affinities of the inhibitors to the various proteases, give some information about the role of the inhibitors in vivo, both in adult and in neonatal pigs.
(Less)
- author
- Ohlsson, Bertil G. ; WestrÖm, Björn R. LU and Karlsson, Börje W. LU
- organization
- publishing date
- 1982-08-10
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- (Pig serum, Colostrum), Chymotrypsin, Elastase, Protease inhibitor, Trypsin
- in
- Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
- volume
- 705
- issue
- 3
- pages
- 9 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:0020479447
- pmid:6181813
- ISSN
- 0167-4838
- DOI
- 10.1016/0167-4838(82)90258-8
- language
- English
- LU publication?
- yes
- id
- 5c0e3451-54e0-44ee-b155-b79582d294c6
- date added to LUP
- 2024-12-05 15:18:28
- date last changed
- 2025-05-08 13:05:34
@article{5c0e3451-54e0-44ee-b155-b79582d294c6,
abstract = {{<p>The partition of <sup>125</sup>I-labelled pancreatic trypsin, chymotrypsin and elastase between the inhibitors, α<sub>2</sub>-macroglobulin f and s, α<sub>1</sub>-protease inhibitor, α<sub>2</sub>-antitrypsin, inter-α-trypsin inhibitor and the specific sow colostrum protease inhibitor, was studied in vitro by gradually increasing the concentration of these proteases in blood serum from adult and newborn pigs. As revealed by immunoelectrophoresis in combination with autoradíography, dífferences were noted in the abilities of the various protease inhibitors to interact with and to form complexes with the three proteases, resulting in changes in location, height and numbers of precipitates. Among the serum inhibitors, α<sub>2</sub>-macroglobulins showed the highest relative affinity to all three proteases, while α<sub>1</sub>-protease inhibitor showed a high relative affinity only for chymotrypsin. Serum α<sub>2</sub>-antitrypsin complexed only with trypsin, with a low relative affinity, α<sub>2</sub>-Antitrypsin also interacted with chymotrypsin and elastase, but without forming complexes. When complexes of sow colostrum protease inhibitor and trypsin were added to the serum from neonatal pigs, these complexes remained stable. The results obtained from these in vitro studies, indicating differences in the relative affinities of the inhibitors to the various proteases, give some information about the role of the inhibitors in vivo, both in adult and in neonatal pigs.</p>}},
author = {{Ohlsson, Bertil G. and WestrÖm, Björn R. and Karlsson, Börje W.}},
issn = {{0167-4838}},
keywords = {{(Pig serum, Colostrum); Chymotrypsin; Elastase; Protease inhibitor; Trypsin}},
language = {{eng}},
month = {{08}},
number = {{3}},
pages = {{357--365}},
publisher = {{Elsevier}},
series = {{Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular}},
title = {{In vitro interaction of porcine serum and colostrum protease inhibitors with pancreatic trypsin, chymotrypsin and elastase}},
url = {{http://dx.doi.org/10.1016/0167-4838(82)90258-8}},
doi = {{10.1016/0167-4838(82)90258-8}},
volume = {{705}},
year = {{1982}},
}