|Vol. 18 >C. Research Notes>III. Genetics of physiological traits and others|
|21.||Genetic variation of glutelin seed storage protein in Myanmar local rice cultivars|
|PA PA AUNG, T. KUMAMARU and H. SATOH
Laboratory of Plant Genetic Resources, Kyushu University, Faculty of Agriculture, Hakozaki, Fukuoka, 812-8581 Japan
Seed storage protein diversity is important for breeding improved nutritional
quality of rice and for the varietal identification. Rice glutelin is
composed of two major subunits: an acidic subunit (alpha subunit) with
molecular mass of 40 kD and a basic subunit (beta subunit) with molecular
mass of 20 kD (Wen and Luthe 1985; Krishnan and Okita 1986). This paper
deals with the genetic variation of a seed storage protein, glutelin,
observed in Myanmar local rice cultivars.
was the same as Kinmaze (lane 1); type 2 had an extra band in the acidic position while the other bands of type 2 were the same as Kinmaze (lane 2). Type 3 was the same as IR36 (lane 3). Type 4 showed that bands 1 and 6 were present but bands 2, A and B were absent (lane 4). In type 5, bands 5 and 6 were present (lane 5). Some variations were also found in the site of glutelin beta subunit. Bands A and B of glutelin beta subunit were found in Kinmaze but not in IR36. However, these bands were also found in type 6 while the other bands of type 6 were the same as IR36 (lane 6). Frequencies of type 1 to 6 were 0.6%, 0.6%, 81%, 0.6%, 1.2% and 16% of total cultivars, respectively. This data indicates that types 2, 4, 5 and 6 of Myanmar local rice cultivars, which were different from that of Kinmaze and IR36, may be recombinant between IR36 type and Kinmaze type. IEF types 1, 2, 3, 4, 5 and 6 were found in SDS-PAGE type A, while IEF types 3, 5 and 6 were observed in type B. Myanmar local rice cultivars were different from the band patterns of typical varieties (Kinmaze and IR36). However, IEF band patterns of Myanmar local rice cultivars showed overlapping variation. The result indicates that Myanmar local rice cultivars are widely diverse in glutelin seed storage protein by IEF analysis.
Brinegar, AC., and DM. Peterson, 1982. Separation and characterization for oat globulin polypeptides. Arch. Biochem. Biophys. 219: 71-79.
Krishnan, H.B. and T.W. Okita, 1986. Structural relationship among the rice glutelin Polypeptides. Plant Physiol. 81: 748-753.
Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of Bacteriophage T4. Nature 227: 680-685.
Wen, T.H., and D.S. Luthe, 1985. Biochemical characterization of rice glutelin. Plant Physiol. 78: 172-177.
|Vol. 18>C. Research Notes> III. Genetics of physiological traits and others|