1995 Volume 64 Issue 3 Pages 471-478
This paper describes a series of style-specific proteins corresponding to five self-incompatibility alleles (S-protein), S1S5, in the Japanese pear (Pyrus serotina Rehd. culta Rehd.). Stylar proteins from various cultivars including a few unclassified S-genotypes were analyzed by isoelectricfocusing polyacrylamide gel electrophoresis (IEF-PAGE).
The S-proteins were focused at the cathodic end of the gel when separated by IEFPAGE using pH 3.59.5 ampholines. The pls of these proteins were quite high, and each protein band was arranged from a cathodic end in the following order: S1, S4, S2, S5 and S3. This order was different from that reported by Sassa et al. (1992, 1993). The Si-, S5- and S3-band were densely stained with CBB (Coomassie Brilliant Blue) ; whereas the S2' and S4-band were lightly stained, especially that of the S2-band. 'Atago' (S2S5) and 'Mat- sukaze' (S-genotype not identified) did not have any S-protein bands in the basic zone of the gel, suggesting that several S-allele associated proteins are present in the neutral or acidic zones of the gel.
Each S-protein band exhibited ribonuclease (RNase) activity, though the activity was far weaker than in those proteins focused in the acidic zone of the IEF-PAGE gel.