Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) II

Detalhes bibliográficos
Autor(a) principal: Beirão,Luiz Henrique
Data de Publicação: 2001
Outros Autores: Mackie,Ian Mckintoch, Teixeira,Evanilda, Damian,César
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Archives of Biology and Technology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132001000100005
Resumo: A trypsin -like enzyme from the pyloric caeca of cod (Gadus morhua) was purified by affinity chromatography on CHOM Sepharose 4B. Some characteristics were established by its catalytic activity on T.A.M.E., typical enzyme substrate, and serine protease inhibitors. The enzyme had an isoelectric point of 5.30 and 5.89 and was very similar in amino acid composition to bovine trypsin, but differed in having a higher relative amount of acidic amino acids and a lower amount of basic amino acids. The enzyme also hydrolysed fish protein substrates.
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spelling Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) IICodenzymetrypsinA trypsin -like enzyme from the pyloric caeca of cod (Gadus morhua) was purified by affinity chromatography on CHOM Sepharose 4B. Some characteristics were established by its catalytic activity on T.A.M.E., typical enzyme substrate, and serine protease inhibitors. The enzyme had an isoelectric point of 5.30 and 5.89 and was very similar in amino acid composition to bovine trypsin, but differed in having a higher relative amount of acidic amino acids and a lower amount of basic amino acids. The enzyme also hydrolysed fish protein substrates.Instituto de Tecnologia do Paraná - Tecpar2001-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132001000100005Brazilian Archives of Biology and Technology v.44 n.1 2001reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132001000100005info:eu-repo/semantics/openAccessBeirão,Luiz HenriqueMackie,Ian MckintochTeixeira,EvanildaDamian,Césareng2001-10-25T00:00:00Zoai:scielo:S1516-89132001000100005Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2001-10-25T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false
dc.title.none.fl_str_mv Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) II
title Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) II
spellingShingle Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) II
Beirão,Luiz Henrique
Cod
enzyme
trypsin
title_short Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) II
title_full Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) II
title_fullStr Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) II
title_full_unstemmed Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) II
title_sort Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) II
author Beirão,Luiz Henrique
author_facet Beirão,Luiz Henrique
Mackie,Ian Mckintoch
Teixeira,Evanilda
Damian,César
author_role author
author2 Mackie,Ian Mckintoch
Teixeira,Evanilda
Damian,César
author2_role author
author
author
dc.contributor.author.fl_str_mv Beirão,Luiz Henrique
Mackie,Ian Mckintoch
Teixeira,Evanilda
Damian,César
dc.subject.por.fl_str_mv Cod
enzyme
trypsin
topic Cod
enzyme
trypsin
description A trypsin -like enzyme from the pyloric caeca of cod (Gadus morhua) was purified by affinity chromatography on CHOM Sepharose 4B. Some characteristics were established by its catalytic activity on T.A.M.E., typical enzyme substrate, and serine protease inhibitors. The enzyme had an isoelectric point of 5.30 and 5.89 and was very similar in amino acid composition to bovine trypsin, but differed in having a higher relative amount of acidic amino acids and a lower amount of basic amino acids. The enzyme also hydrolysed fish protein substrates.
publishDate 2001
dc.date.none.fl_str_mv 2001-03-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132001000100005
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132001000100005
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1516-89132001000100005
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
publisher.none.fl_str_mv Instituto de Tecnologia do Paraná - Tecpar
dc.source.none.fl_str_mv Brazilian Archives of Biology and Technology v.44 n.1 2001
reponame:Brazilian Archives of Biology and Technology
instname:Instituto de Tecnologia do Paraná (Tecpar)
instacron:TECPAR
instname_str Instituto de Tecnologia do Paraná (Tecpar)
instacron_str TECPAR
institution TECPAR
reponame_str Brazilian Archives of Biology and Technology
collection Brazilian Archives of Biology and Technology
repository.name.fl_str_mv Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)
repository.mail.fl_str_mv babt@tecpar.br||babt@tecpar.br
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