Hostname: page-component-cd9895bd7-dk4vv Total loading time: 0 Render date: 2024-12-18T23:04:42.793Z Has data issue: false hasContentIssue false
  • English
  • Français

α-Amylase isoenzymes and BASI-like proteins in seeds of different grass species

Published online by Cambridge University Press:  19 September 2008

C. A. Cornford  and
R. D. Hill
C. A. Cornford
Affiliation:
Department of Plant Biology and Biotechnology, Massey University, Palmerston North, New Zealand.
R. D. Hill*
Affiliation:
Department of Plant Science, University of Manitoba, Winnipeg, Manitoba, R3T 2N2, Canada
*
* Correspondence
Get access Rights & Permissions [Opens in a new window]

Abstract

Seeds from an assortment of 28 grass species (including two cereals), chiefly representing different tribes of the sub-family Pooideae were tested for the presence of BASI-like proteins using Western blotting techniques and antisera raised against the barley amylase/subtilisin inhibitor. A single protein species of the same molecular weight as the BASI protein was detected in each member of the tribes Triticeae and Bromeae tested. Members of the Triticeae and Bromeae were the only species to produce high pi α-amylase isoenzymes following germination of the grain in addition to low pl forms which were present in all species tested. Anti-BASI antibody binding patterns for the other grasses examined were variable with the strongest staining being observed for Lolium species. In these species, either a double or single protein band fractionally larger than the BASI protein was recognized. In most other cases antibody binding was barely or not detectable. Inhibitor preparations from Hordeum vulgare and Lolium perenne were effective at inhibiting wheat α-amylase but neither had any effect against enzyme produced by germinating L. perenne.

Keywords

α-amylase isoenzymesBASIcereal and grass seedPooideae
Type
Research Papers
Information
Seed Science Research , Volume 4 , Issue 3 , September 1994 , pp. 285 - 291
Copyright
Copyright © Cambridge University Press 1994

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Aisen, A.O. and Palmer, G.H. (1983) The sorghum embryo in relation to the hydrolysis of the endosperm during germination and seedling growth. Journal of the Science of Food and Agriculture, 34, 113–121.CrossRefGoogle Scholar
Aisien, A.O., Palmer, G.H. and Stark, J.R. (1983) The development of enzymes during germination and seedling growth in Nigerian sorghum. Stärke 35, 316–320.CrossRefGoogle Scholar
Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248–254.Google Scholar
Briggs, D.E. (1961) A modification of the Sandstedt, Kneen and Blish assay of α-amylase. Journal of the Institute of Brewing 67, 427–431.CrossRefGoogle Scholar
Clayton, W.D. and Renvoise, S.E. (1976) Genera Graminum. H.M. Stationery Office, London.Google Scholar
Cornford, C.A., Black, M., Daussant, J. and Murdoch, K.M. (1987) α-Amylase production by premature wheat (Triticum aestivum L.) embryos. Journal of Experimental Botany 38, 277–285.CrossRefGoogle Scholar
Fincher, G.B. (1989) Molecular and cellular biology associated with endosperm mobilisation in germinating cereal grains. Annual Review of Plant Physiology and Plant Molecular Biology 40, 305–346.CrossRefGoogle Scholar
Harlow, E. and Lane, D. (1988) Antibodies, a laboratory guide. p. 505,New York, USA, Cold Spring Harbour Laboratories.Google Scholar
Hejgaard, J., Bjorn, S.E. and Neilsen, G. (1984) Rye chromosomes carrying structural genes for the major grain protease inhibitors. Heriditas 101, 257–286.CrossRefGoogle Scholar
Henry, R.J., Battershell, V.G., Brennan, P.S. and Oono, K. (1992) Control of wheat α-amylase using inhibitors from cereals. Journal of the Science of Food and Agriculture 58, 281–284.CrossRefGoogle Scholar
Hill, R.D. and MacGregor, A.W. (1988) Cereal α-amylases in grain research and technology. Advances in Cereal Science and Technology 9, 217–265.Google Scholar
Hill, R.D., Gubbels, S., Sumner, M. and MacGregor, A.W. (1993) Regulation of starch breakdown in cereal caryopses. pp 143–152in Côme, D. and Corbineau, F. (Eds) Basic and applied aspects of seed biology, Fourth International Workshop on Seeds, Angers. Saint-Denis, France, De Brabanter.Google Scholar
Hill, R.D., Weselake, R.J., Macgregor, A.W. and Daussant, J. (1987) A review of some of the properties of an endogenous inhibitor of cereal alpha-amylase. pp 474–482in Mares, D.J. (Ed.) Fourth International Symposium on Pre-harvest Sprouting in Cereals. Boulder, Colorado, Westview Press.Google Scholar
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.CrossRefGoogle ScholarPubMed
Leah, R. and Mundy, J. (1989) The bifunctional α-amylase/subtilisin inhibitor of barley: nucleotide sequence and patterns of seed specific expression. Plant Molecular Biology 12, 673–682.CrossRefGoogle ScholarPubMed
MacGregor, A.W. (1976) A note on the formation of α-amylase in de-embryonated barley kernels. Cereal Chemistry 53, 792–796.Google Scholar
MacGregor, A.W. and Ballance, D.L. (1980) Hydrolysis of large and small starch granules from normal and waxy barley cultivars by α-amylase from barley malt. Cereal Chemistry 57, 397–402.Google Scholar
MacGregor, A.W. and Marchylo, B.A. (1986) α-Amylase components in excised, incubated barley embryos. Journal of the Institute of Brewing 92, 159–161.CrossRefGoogle Scholar
MacGregor, A.W. and Morgan, J.E. (1986) Hydrolysis of barley starch granules by α-amylase from barley malt. Cereal Foods World 31, 688–693.Google Scholar
MacGregor, A.W. and Morgan, J.E. (1992) Determination of specific activities of malt α-amylases. Journal of Cereal Science 16, 267–277.CrossRefGoogle Scholar
Marchylo, B.A., MacGregor, A.W. and Kruger, J.E. (1987) Quantitative analysis of multiple forms of α-amylase produced in germinating cereals. pp 522–533in Mares, D.J. (Ed.) Fourth International Symposium on Pre-harvest Sprouting in Cereals. Boulder, Colorado, Westview Press.Google Scholar
Mundy, J., Svendsen, I. and Hejgaard, J. (1983) Barley α-amylase/subtilisin inhibitor. I. Isolation and characterisation. Carlsberg Research Communication 48, 81–90.CrossRefGoogle Scholar
Mundy, J., Hejgaard, J. and Svendsen, I. (1984) Characterisation of a bifunctional wheat inhibitor of endogenous α-amylase and subtilisin. FEBS Letters 167, 210–214.Google Scholar
Okamoto, K., Kitano, H. and Akazawa, T. (1980) Biosynthesis and excretion of hydrolases in germinating cereal seeds. Plant Cell Physiology 21, 201–204.Google Scholar
Silvanovich, M.P. and Hill, R.D. (1976) Affinity chromatography of cereal α-amylase. Analytical Biochemistry 73, 430–433.Google Scholar
Svendsen, I., Hejgaard, J. and Mundy, J. (1986) Complete amino acid sequence of the α-amylase/subtilisin inhibitor from barley. Carlsberg Research Communication 51, 43–50.CrossRefGoogle Scholar
Watson, L. and Dallwitz, M.J. (1992) The grass genera of the world. Wallingford, CAB International.Google Scholar
Weselake, R.J., MacGregor, A.W. and Hill, R.D. (1983a) An endogenous α-amylase inhibitor in barley kernels. Plant Physiology 72, 809–812.CrossRefGoogle ScholarPubMed
Weselake, R.J., MacGregor, A.W. and Hill, R.D. (1983b) Purification and characteristics of an endogenous α-amylase inhibitor from barley kernels. Plant Physiology 73, 1008–1012.CrossRefGoogle ScholarPubMed
Weselake, R.J., MacGregor, A.W. and Hill, R.D. (1985) Endogenous α-amylase inhibitor in various cereals. Cereal Chemistry 62, 120–123.Google Scholar