Enzyme action as bearing on the validity of the ionic-dissociation hypothesis and on the phenomena of vital change

Autores
Armstrong, Henry E.
Año de publicación
1904
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
In discussing the changes which attend fermentation, I pointed out, in 1895, that “Such changes are known to occur entirely within the cell and are presumably functions of the protoplasm; in other words, they probably occur within very complex molecular systems of extreme instability, perhaps under the influence of, in contact with, the very same hydrolyst (enzyme) which is so active, when separated from the cell, in promoting the hydrolysis of cane sugar; or if not, of substances of a similar nature.” This explanation has gained greatly in prob­ ability now that it is established that the sucroclastic enzymes are very closely related to the alcoholic ferments.
Material digitalizado en SEDICI en colaboración con la Biblioteca de Física de la Facultad de Ciencias Exactas (UNLP).
Biblioteca del Departamento de Física
Materia
Química
Enzimas
Glucosamina
Carbohidratos
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/publicdomain/mark/1.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/29295

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network_name_str SEDICI (UNLP)
spelling Enzyme action as bearing on the validity of the ionic-dissociation hypothesis and on the phenomena of vital changeArmstrong, Henry E.QuímicaEnzimasGlucosaminaCarbohidratosIn discussing the changes which attend fermentation, I pointed out, in 1895, that “Such changes are known to occur entirely within the cell and are presumably functions of the protoplasm; in other words, they probably occur within very complex molecular systems of extreme instability, perhaps under the influence of, in contact with, the very same hydrolyst (enzyme) which is so active, when separated from the cell, in promoting the hydrolysis of cane sugar; or if not, of substances of a similar nature.” This explanation has gained greatly in prob­ ability now that it is established that the sucroclastic enzymes are very closely related to the alcoholic ferments.Material digitalizado en SEDICI en colaboración con la Biblioteca de Física de la Facultad de Ciencias Exactas (UNLP).Biblioteca del Departamento de Física1904info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf537-542http://sedici.unlp.edu.ar/handle/10915/29295enginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/publicdomain/mark/1.0/Creative Public Domainreponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-10T12:00:40Zoai:sedici.unlp.edu.ar:10915/29295Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-10 12:00:40.636SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Enzyme action as bearing on the validity of the ionic-dissociation hypothesis and on the phenomena of vital change
title Enzyme action as bearing on the validity of the ionic-dissociation hypothesis and on the phenomena of vital change
spellingShingle Enzyme action as bearing on the validity of the ionic-dissociation hypothesis and on the phenomena of vital change
Armstrong, Henry E.
Química
Enzimas
Glucosamina
Carbohidratos
title_short Enzyme action as bearing on the validity of the ionic-dissociation hypothesis and on the phenomena of vital change
title_full Enzyme action as bearing on the validity of the ionic-dissociation hypothesis and on the phenomena of vital change
title_fullStr Enzyme action as bearing on the validity of the ionic-dissociation hypothesis and on the phenomena of vital change
title_full_unstemmed Enzyme action as bearing on the validity of the ionic-dissociation hypothesis and on the phenomena of vital change
title_sort Enzyme action as bearing on the validity of the ionic-dissociation hypothesis and on the phenomena of vital change
dc.creator.none.fl_str_mv Armstrong, Henry E.
author Armstrong, Henry E.
author_facet Armstrong, Henry E.
author_role author
dc.subject.none.fl_str_mv Química
Enzimas
Glucosamina
Carbohidratos
topic Química
Enzimas
Glucosamina
Carbohidratos
dc.description.none.fl_txt_mv In discussing the changes which attend fermentation, I pointed out, in 1895, that “Such changes are known to occur entirely within the cell and are presumably functions of the protoplasm; in other words, they probably occur within very complex molecular systems of extreme instability, perhaps under the influence of, in contact with, the very same hydrolyst (enzyme) which is so active, when separated from the cell, in promoting the hydrolysis of cane sugar; or if not, of substances of a similar nature.” This explanation has gained greatly in prob­ ability now that it is established that the sucroclastic enzymes are very closely related to the alcoholic ferments.
Material digitalizado en SEDICI en colaboración con la Biblioteca de Física de la Facultad de Ciencias Exactas (UNLP).
Biblioteca del Departamento de Física
description In discussing the changes which attend fermentation, I pointed out, in 1895, that “Such changes are known to occur entirely within the cell and are presumably functions of the protoplasm; in other words, they probably occur within very complex molecular systems of extreme instability, perhaps under the influence of, in contact with, the very same hydrolyst (enzyme) which is so active, when separated from the cell, in promoting the hydrolysis of cane sugar; or if not, of substances of a similar nature.” This explanation has gained greatly in prob­ ability now that it is established that the sucroclastic enzymes are very closely related to the alcoholic ferments.
publishDate 1904
dc.date.none.fl_str_mv 1904
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://sedici.unlp.edu.ar/handle/10915/29295
url http://sedici.unlp.edu.ar/handle/10915/29295
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/publicdomain/mark/1.0/
Creative Public Domain
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rights_invalid_str_mv http://creativecommons.org/publicdomain/mark/1.0/
Creative Public Domain
dc.format.none.fl_str_mv application/pdf
537-542
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instname:Universidad Nacional de La Plata
instacron:UNLP
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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