Abstract
An assay has been developed to measure protease activity in endosperm extracts of maize seeds. With hemoglobin as substrate, the enzyme(s) has a pH optimum of 3.8 and a temperature optimum of 46 C. It also degrades gliadin, edestin, bovine serum albumin, and partially hydrolyzed zein and glutelin under standard assay conditions. The enzyme(s) has endopeptidase activity with all substrates tested. When undenatured zein and glutelin are suspended in an agar gel, both are efficiently degraded. Using this assay, the protease activity increases from day 3 to day 8 after inhibition and then declines.
Full text
PDFImages in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Harvey B. M., Oaks A. The Hydrolysis of Endosperm Protein in Zea mays. Plant Physiol. 1974 Mar;53(3):453–457. doi: 10.1104/pp.53.3.453. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Jacobsen J. V., Varner J. E. Gibberellic Acid-induced synthesis of protease by isolated aleurone layers of barley. Plant Physiol. 1967 Nov;42(11):1596–1600. doi: 10.1104/pp.42.11.1596. [DOI] [PMC free article] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Ory R. L., Henningsen K. W. Enzymes associated with protein bodies isolated from ungerminated barley seeds. Plant Physiol. 1969 Nov;44(11):1488–1498. doi: 10.1104/pp.44.11.1488. [DOI] [PMC free article] [PubMed] [Google Scholar]