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. 1971 May;47(5):629–634. doi: 10.1104/pp.47.5.629

An Invertase Inactivator in Maize Endosperm and Factors Affecting Inactivation 1,2

T A Jaynes a,3, O E Nelson a,4
PMCID: PMC396740  PMID: 16657674

Abstract

A protein present in the developing endosperm of maize (Zea mays L.) causes a loss of invertase activity under certain conditions of incubation. This protein, designated an inactivator, inactivates invertase I of maize even in the presence of other proteins. No inactivation of invertase II of maize or yeast invertase has been observed. The inactivator and invertase I are found only in the endosperm. The quantity of inactivator increases in the normal endosperm during development while invertase I activity decreases. However, the altered levels of invertase I activity in several endosperm mutant lines do not result from different quantities of inactivator. The inactivator can decrease invertase I activity during a preincubation period before addition of sucrose; inactivation is noncompetitive. Invertase I activity decreases curvilinearly with an increase in inactivator concentration. At high buffer concentrations or low inactivator concentrations in the reaction mixture, a latent period is observed when invertase I is not inactivated. Inactivation increases with an increase in temperature and a decrease in pH.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Jaynes T. A., Nelson O. E. Invertase Activity in Normal and Mutant Maize Endosperms during Development. Plant Physiol. 1971 May;47(5):623–628. doi: 10.1104/pp.47.5.623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Pressey R. Invertase inhibitor from potatoes: purification, characterization, and reactivity with plant invertases. Plant Physiol. 1967 Dec;42(12):1780–1786. doi: 10.1104/pp.42.12.1780. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Pressey R. Separation and properties of potato invertase and invertase inhibitor. Arch Biochem Biophys. 1966 Mar;113(3):667–674. doi: 10.1016/0003-9861(66)90246-3. [DOI] [PubMed] [Google Scholar]
  4. Pressey R., Shaw R. Effect of temperature on invertase, invertase inhibitor, and sugars in potato tubers. Plant Physiol. 1966 Dec;41(10):1657–1661. doi: 10.1104/pp.41.10.1657. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. SCHIMKE R. T. THE IMPORTANCE OF BOTH SYNTHESIS AND DEGRADATION IN THE CONTROL OF ARGINASE LEVELS IN RAT LIVER. J Biol Chem. 1964 Nov;239:3808–3817. [PubMed] [Google Scholar]
  6. SCHLESINGER M. J. IN VITRO COMPLEMENTATION AND THE SUBUNIT STRUCTURE OF E. COLI ALKALINE PHOSPHATASE. Brookhaven Symp Biol. 1964 Dec;17:66–79. [PubMed] [Google Scholar]
  7. SCHLESINGER M. J., LEVINTHAL C. Hybrid protein formation of E. coli alkaline phosphatase leading to in vitro complementation. J Mol Biol. 1963 Jul;7:1–12. doi: 10.1016/s0022-2836(63)80014-5. [DOI] [PubMed] [Google Scholar]
  8. SWICK R. W. Measurement of protein turnover in rat liver. J Biol Chem. 1958 Apr;231(2):751–764. [PubMed] [Google Scholar]
  9. Zucker M. Sequential Induction of Phenylalanine Ammonia-lyase and a Lyase-inactivating System in Potato Tuber Disks. Plant Physiol. 1968 Mar;43(3):365–374. doi: 10.1104/pp.43.3.365. [DOI] [PMC free article] [PubMed] [Google Scholar]

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