New α-amylase and trypsin inhibitors among the CM-proteins of barley (Hordeum vulgare)

Barber, Domingo; Sánchez-Monge Laguna de Rins, Rosa; Mendez, Enrique; Lazaro, Ana; García Olmedo, Francisco y Salcedo Duran, Gabriel (1986). New α-amylase and trypsin inhibitors among the CM-proteins of barley (Hordeum vulgare). "Biochimica et Biophysica Acta", v. 869 (n. 1); pp. 115-118. ISSN 0167-4838. https://doi.org/10.1016/0167-4838(86)90318-3.

Descripción

Título: New α-amylase and trypsin inhibitors among the CM-proteins of barley (Hordeum vulgare)
Autor/es:
  • Barber, Domingo
  • Sánchez-Monge Laguna de Rins, Rosa
  • Mendez, Enrique
  • Lazaro, Ana
  • García Olmedo, Francisco
  • Salcedo Duran, Gabriel
Tipo de Documento: Artículo
Título de Revista/Publicación: Biochimica et Biophysica Acta
Fecha: Enero 1986
Volumen: 869
Materias:
Palabras Clave Informales: α-Amylase inhibitor; Trypsin inhibitor; Amino acid sequence; (Barley endosperm)
Escuela: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Departamento: Biotecnologia [hasta 2014]
Licencias Creative Commons: Reconocimiento - Sin obra derivada - No comercial

Texto completo

[img]
Vista Previa
PDF (Document Portable Format) - Se necesita un visor de ficheros PDF, como GSview, Xpdf o Adobe Acrobat Reader
Descargar (150kB) | Vista Previa

Resumen

Barley CM-proteins are a group of at least five salt-soluble components (CMa-e) that can be selectively extracted from endosperm with chloroform/methanol mixtures. N-terminal sequences of proteins CMa, CMb and CMc have been determined and found to be homologous to those previously determined for CMd and CMc, an observation which confirms that their structural genes are members of a dispersed multi-gene family. The purified CM-proteins were tested against trypsin and against α-amylases from saliva, pancreas, Aspergillus oryzae, Tenebrio molitor and barley. Besides CMe, which was known to be a trypsin inhibitor, CMc also showed antitrypsin activity, whereas CMa was specifically active against the α-amylase from T. molitor and no inhibitory activity was found for proteins CMb and CMd. The evolutionary implications of these findings are discussed

Más información

ID de Registro: 5889
Identificador DC: http://oa.upm.es/5889/
Identificador OAI: oai:oa.upm.es:5889
Identificador DOI: 10.1016/0167-4838(86)90318-3
URL Oficial: http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6T21-47T33JM-N&_user=885385&_coverDate=01/17/1986&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_acct=C000047350&_version=1&_urlVersion=0&_userid=885385&md5=4f7d5505dac25
Depositado por: Memoria Investigacion
Depositado el: 03 Feb 2011 12:28
Ultima Modificación: 20 Abr 2016 14:35
  • Open Access
  • Open Access
  • Sherpa-Romeo
    Compruebe si la revista anglosajona en la que ha publicado un artículo permite también su publicación en abierto.
  • Dulcinea
    Compruebe si la revista española en la que ha publicado un artículo permite también su publicación en abierto.
  • Recolecta
  • e-ciencia
  • Observatorio I+D+i UPM
  • OpenCourseWare UPM