Purification and Partial Characterization of a Dipeptidase from Barley 1
AUTOR(ES)
Sopanen, Tuomas
RESUMO
A peptidase hydrolyzing the dipeptide Ala-Gly optimally at pH 8 to 9 was purified about 3500-fold from germinated grains of barley (Hordeum vulgare L.). According to disc electrophoresis in the presence of sodium dodecyl sulfate, the preparation was about 90% pure.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=542137Documentos Relacionados
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