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Release of dog polymorphonuclear leukocyte cathepsin g, normally and in endotoxin and pancreatitic shock : Isolation and partial characterization of dog polymorphonuclear leukocyte cathepsin g

Björk, Peter LU ; Axelsson, Lena LU and Ohlsson, Kjell (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

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Please use this url to cite or link to this publication:
author
organization
publishing date
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
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
2017-03-26 04:50:42
@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. &amp; by Walter de Gruyter &amp; Co</p>},
  author       = {Björk, Peter and Axelsson, Lena and Ohlsson, Kjell},
  issn         = {0177-3593},
  keyword      = {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},
  volume       = {372},
  year         = {1991},
}