Release of dog polymorphonuclear leukocyte cathepsin g, normally and in endotoxin and pancreatitic shock : Isolation and partial characterization of dog polymorphonuclear leukocyte cathepsin g
(1991) In Biological Chemistry Hoppe-Seyler 372(1). p.419-426- Abstract
Dog polymorphonuclear leukocyte cathepsin G was isolated from a granule extract using a two-step procedure including affinity chromatography on aTrasylol-Sepharose gel and ion-exchange chromatography on a CM 52 column. 22 of the first 24 N-terminal amino acids were determined and showed 83% and 71% identity to those of human and rat cathepsin G, respectively. Total amino-acid composition demonstrated the basic nature of the protein. In an SDS/polyacrylamide-gel electrophoresis the protein showed an Mr of 29400 compared to the Mr of 26800 calculated from the total amino-acid composition. The enzyme was shown to form complexes with α1α2-macroglobulin and arproteinase inhibitor. A specific enzyme-linked immunosorbent assay was developed... (More)
Dog polymorphonuclear leukocyte cathepsin G was isolated from a granule extract using a two-step procedure including affinity chromatography on aTrasylol-Sepharose gel and ion-exchange chromatography on a CM 52 column. 22 of the first 24 N-terminal amino acids were determined and showed 83% and 71% identity to those of human and rat cathepsin G, respectively. Total amino-acid composition demonstrated the basic nature of the protein. In an SDS/polyacrylamide-gel electrophoresis the protein showed an Mr of 29400 compared to the Mr of 26800 calculated from the total amino-acid composition. The enzyme was shown to form complexes with α1α2-macroglobulin and arproteinase inhibitor. A specific enzyme-linked immunosorbent assay was developed for the determination of cathepsin G/α proteinase inhibitor complex in dog plasma and tissue fluids. The mean concentration of cathepsin G in normal dog plasma was determined to be 38 μ/l, measured as cathepsin G/α1-proteinase inhibitor complex. When active dog cathepsin G was added to normal dog plasma in vitro, approximately 56% could be measured by the assay. Slow intravenous infusion of a lethal dose of endotoxin in dogs was followed by a marked drop in white blood cell count and thrombocytes and a simultaneous rapid increase in plasma cathepsin G concentration, reaching a maximum level of 150 β/l. Bile-induced experimental pancreatitis in dogs was accompanied by successive increase in cathepsin G levels in plasma as well as in peritoneal exudates, reaching a maximum level of about 300 μ/l in plasma and 18 mg/ l in the exudates during the late stages of disease. & by Walter de Gruyter & Co
(Less)
- author
- Björk, Peter LU ; Axelsson, Lena LU and Ohlsson, Kjell
- organization
- publishing date
- 1991
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Cathepsin G, endotoxin, pancreatitis, polymorphonuclear leukocytes, shock
- in
- Biological Chemistry Hoppe-Seyler
- volume
- 372
- issue
- 1
- pages
- 8 pages
- publisher
- De Gruyter
- external identifiers
-
- scopus:0026177184
- pmid:1910580
- ISSN
- 0177-3593
- DOI
- 10.1515/bchm3.1991.372.1.419
- language
- English
- LU publication?
- yes
- id
- 40739ca1-630a-498f-94cf-ff652bbfa039
- date added to LUP
- 2017-03-10 13:37:41
- date last changed
- 2024-01-13 16:48:33
@article{40739ca1-630a-498f-94cf-ff652bbfa039, abstract = {{<p>Dog polymorphonuclear leukocyte cathepsin G was isolated from a granule extract using a two-step procedure including affinity chromatography on aTrasylol-Sepharose gel and ion-exchange chromatography on a CM 52 column. 22 of the first 24 N-terminal amino acids were determined and showed 83% and 71% identity to those of human and rat cathepsin G, respectively. Total amino-acid composition demonstrated the basic nature of the protein. In an SDS/polyacrylamide-gel electrophoresis the protein showed an Mr of 29400 compared to the Mr of 26800 calculated from the total amino-acid composition. The enzyme was shown to form complexes with α1α2-macroglobulin and arproteinase inhibitor. A specific enzyme-linked immunosorbent assay was developed for the determination of cathepsin G/α proteinase inhibitor complex in dog plasma and tissue fluids. The mean concentration of cathepsin G in normal dog plasma was determined to be 38 μ/l, measured as cathepsin G/α1-proteinase inhibitor complex. When active dog cathepsin G was added to normal dog plasma in vitro, approximately 56% could be measured by the assay. Slow intravenous infusion of a lethal dose of endotoxin in dogs was followed by a marked drop in white blood cell count and thrombocytes and a simultaneous rapid increase in plasma cathepsin G concentration, reaching a maximum level of 150 β/l. Bile-induced experimental pancreatitis in dogs was accompanied by successive increase in cathepsin G levels in plasma as well as in peritoneal exudates, reaching a maximum level of about 300 μ/l in plasma and 18 mg/ l in the exudates during the late stages of disease. & by Walter de Gruyter & Co</p>}}, author = {{Björk, Peter and Axelsson, Lena and Ohlsson, Kjell}}, issn = {{0177-3593}}, keywords = {{Cathepsin G; endotoxin; pancreatitis; polymorphonuclear leukocytes; shock}}, language = {{eng}}, number = {{1}}, pages = {{419--426}}, publisher = {{De Gruyter}}, series = {{Biological Chemistry Hoppe-Seyler}}, title = {{Release of dog polymorphonuclear leukocyte cathepsin g, normally and in endotoxin and pancreatitic shock : Isolation and partial characterization of dog polymorphonuclear leukocyte cathepsin g}}, url = {{http://dx.doi.org/10.1515/bchm3.1991.372.1.419}}, doi = {{10.1515/bchm3.1991.372.1.419}}, volume = {{372}}, year = {{1991}}, }