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

Barber, Domingo and Sánchez-Monge Laguna de Rins, Rosa and Mendez, Enrique and Lazaro, Ana and García Olmedo, Francisco and 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.

Description

Title: New α-amylase and trypsin inhibitors among the CM-proteins of barley (Hordeum vulgare)
Author/s:
  • Barber, Domingo
  • Sánchez-Monge Laguna de Rins, Rosa
  • Mendez, Enrique
  • Lazaro, Ana
  • García Olmedo, Francisco
  • Salcedo Duran, Gabriel
Item Type: Article
Título de Revista/Publicación: Biochimica et Biophysica Acta
Date: January 1986
ISSN: 0167-4838
Volume: 869
Subjects:
Freetext Keywords: α-Amylase inhibitor; Trypsin inhibitor; Amino acid sequence; (Barley endosperm)
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

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

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