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Purification of a Trypsin Inhibitor Secreted by Embryogenic Carrot Cells

A protease inhibitor with a molecular weight of about 12,800 was purified to electrophoretic homogeneity from Daucus carota cells. The protease inhibitor was heat stable and inhibited trypsin but had no activity toward chymotrypsin or subtilisin. Nonembryogenic as well as embryogenic strains contain...

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Detalles Bibliográficos
Autores principales: Carlberg, Irene, Jonsson, Lisbeth, Bergenstråhle, Annika, Söderhäll, Kenneth
Formato: Artigo
Lenguaje:Inglês
Publicado: 1987
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Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC1056551/
https://ncbi.nlm.nih.gov/pubmed/16665398
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