Interaction of bovine alpha2 macroglobulin with proteinases

Detalhes bibliográficos
Autor(a) principal: Toloi, Maria Regina Torqueti
Data de Publicação: 1994
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Veterinary Research and Animal Science
Texto Completo: https://www.revistas.usp.br/bjvras/article/view/52053
Resumo: The alpha2-macroglobulin (alpha2M) protease inhibitor was purified from bovine plasma. The alpha2M preparations at various purification steps were identified by immunodiffusion and crossed immunoelectrophoresis with anti-human alpha2 serum. Anti-bovine alpha2M serum was prepared for the quantitative determinations. The purest alpha2M preparation was obtained by affinity chromatography and used as primary standard in radial immunodiffusion. Alpha2M preparations were submitted to binding tests with p' - NPGB (p‘ - nitrophenyl-p-guanidinebenzoate HCL) titrated trypsin and plasmin. Alpha2M protected 35% of the esterolytic activity of trypsin and 50% of the amidolytic activity of plasmin.
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spelling Interaction of bovine alpha2 macroglobulin with proteinasesInteração de alpha2 macroglobulina bovina com proteinasesBovinosPlasmaInibidores da proteaseAlpha2MPlasminaTripsinaCattlePlasmaProteinase inhibitorsAlpha2MPlasminTrypsinThe alpha2-macroglobulin (alpha2M) protease inhibitor was purified from bovine plasma. The alpha2M preparations at various purification steps were identified by immunodiffusion and crossed immunoelectrophoresis with anti-human alpha2 serum. Anti-bovine alpha2M serum was prepared for the quantitative determinations. The purest alpha2M preparation was obtained by affinity chromatography and used as primary standard in radial immunodiffusion. Alpha2M preparations were submitted to binding tests with p' - NPGB (p‘ - nitrophenyl-p-guanidinebenzoate HCL) titrated trypsin and plasmin. Alpha2M protected 35% of the esterolytic activity of trypsin and 50% of the amidolytic activity of plasmin.Alpha2 Macroglobulina, uma proteína inibidora de proteases, foi isolada do plasma bovino. O processo de purificação foi monitorado por imunodifusão e imunoeletroforese cruzada com soro anti alpha2M-humana. Para as determinações quantitativas foi preparado um soro anti alpha2M bovino. A preparação mais pura de alpha2M foi obtida por cromatografia de afinidade e usada como padrão primário na imunodifusão radial de Mancini. Preparações de alpha2M foram usadas em testes de ligação com tripsina e plasmina (tituladas com NPGB). Nos testes de ligação 50% de plasmina e 35% de tripsina foram "protegidas” pela alpha2M. Não foi possível determinar se houve ineficiência na ligação ou se a perda de atividade ocorreu por alterações na afinidade do complexo alpha2M-protease, em relação aos substratos usados.Universidade de São Paulo. Faculdade de Medicina Veterinária e Zootecnia1994-06-02info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://www.revistas.usp.br/bjvras/article/view/5205310.11606/issn.1678-4456.bjvras.1994.52053Brazilian Journal of Veterinary Research and Animal Science; Vol. 31 Núm. 2 (1994); 101-105Brazilian Journal of Veterinary Research and Animal Science; Vol. 31 No. 2 (1994); 101-105Brazilian Journal of Veterinary Research and Animal Science; v. 31 n. 2 (1994); 101-105Brazilian Journal of Veterinary Research and Animal Science; V. 31 N. 2 (1994); 101-1051678-44561413-9596reponame:Brazilian Journal of Veterinary Research and Animal Scienceinstname:Faculdade de Medicina Veterinária e Zootecnia da Universidade de São Paulo (FMVZ-USP)instacron:USPenghttps://www.revistas.usp.br/bjvras/article/view/52053/56103Toloi, Maria Regina Torquetiinfo:eu-repo/semantics/openAccess2020-06-23T04:52:58Zoai:revistas.usp.br:article/52053Revistahttps://www.revistas.usp.br/bjvrasPUBhttps://www.revistas.usp.br/bjvras/oaibjvras@usp.br1413-95961413-9596opendoar:https://www.revistas.usp.br/bjvras/index2023-01-12T16:43:28.090233Brazilian Journal of Veterinary Research and Animal Science - Faculdade de Medicina Veterinária e Zootecnia da Universidade de São Paulo (FMVZ-USP)false
dc.title.none.fl_str_mv Interaction of bovine alpha2 macroglobulin with proteinases
Interação de alpha2 macroglobulina bovina com proteinases
title Interaction of bovine alpha2 macroglobulin with proteinases
spellingShingle Interaction of bovine alpha2 macroglobulin with proteinases
Toloi, Maria Regina Torqueti
Bovinos
Plasma
Inibidores da protease
Alpha2M
Plasmina
Tripsina
Cattle
Plasma
Proteinase inhibitors
Alpha2M
Plasmin
Trypsin
title_short Interaction of bovine alpha2 macroglobulin with proteinases
title_full Interaction of bovine alpha2 macroglobulin with proteinases
title_fullStr Interaction of bovine alpha2 macroglobulin with proteinases
title_full_unstemmed Interaction of bovine alpha2 macroglobulin with proteinases
title_sort Interaction of bovine alpha2 macroglobulin with proteinases
author Toloi, Maria Regina Torqueti
author_facet Toloi, Maria Regina Torqueti
author_role author
dc.contributor.author.fl_str_mv Toloi, Maria Regina Torqueti
dc.subject.por.fl_str_mv Bovinos
Plasma
Inibidores da protease
Alpha2M
Plasmina
Tripsina
Cattle
Plasma
Proteinase inhibitors
Alpha2M
Plasmin
Trypsin
topic Bovinos
Plasma
Inibidores da protease
Alpha2M
Plasmina
Tripsina
Cattle
Plasma
Proteinase inhibitors
Alpha2M
Plasmin
Trypsin
description The alpha2-macroglobulin (alpha2M) protease inhibitor was purified from bovine plasma. The alpha2M preparations at various purification steps were identified by immunodiffusion and crossed immunoelectrophoresis with anti-human alpha2 serum. Anti-bovine alpha2M serum was prepared for the quantitative determinations. The purest alpha2M preparation was obtained by affinity chromatography and used as primary standard in radial immunodiffusion. Alpha2M preparations were submitted to binding tests with p' - NPGB (p‘ - nitrophenyl-p-guanidinebenzoate HCL) titrated trypsin and plasmin. Alpha2M protected 35% of the esterolytic activity of trypsin and 50% of the amidolytic activity of plasmin.
publishDate 1994
dc.date.none.fl_str_mv 1994-06-02
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://www.revistas.usp.br/bjvras/article/view/52053
10.11606/issn.1678-4456.bjvras.1994.52053
url https://www.revistas.usp.br/bjvras/article/view/52053
identifier_str_mv 10.11606/issn.1678-4456.bjvras.1994.52053
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv https://www.revistas.usp.br/bjvras/article/view/52053/56103
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidade de São Paulo. Faculdade de Medicina Veterinária e Zootecnia
publisher.none.fl_str_mv Universidade de São Paulo. Faculdade de Medicina Veterinária e Zootecnia
dc.source.none.fl_str_mv Brazilian Journal of Veterinary Research and Animal Science; Vol. 31 Núm. 2 (1994); 101-105
Brazilian Journal of Veterinary Research and Animal Science; Vol. 31 No. 2 (1994); 101-105
Brazilian Journal of Veterinary Research and Animal Science; v. 31 n. 2 (1994); 101-105
Brazilian Journal of Veterinary Research and Animal Science; V. 31 N. 2 (1994); 101-105
1678-4456
1413-9596
reponame:Brazilian Journal of Veterinary Research and Animal Science
instname:Faculdade de Medicina Veterinária e Zootecnia da Universidade de São Paulo (FMVZ-USP)
instacron:USP
instname_str Faculdade de Medicina Veterinária e Zootecnia da Universidade de São Paulo (FMVZ-USP)
instacron_str USP
institution USP
reponame_str Brazilian Journal of Veterinary Research and Animal Science
collection Brazilian Journal of Veterinary Research and Animal Science
repository.name.fl_str_mv Brazilian Journal of Veterinary Research and Animal Science - Faculdade de Medicina Veterinária e Zootecnia da Universidade de São Paulo (FMVZ-USP)
repository.mail.fl_str_mv bjvras@usp.br
_version_ 1797051563844304896

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