Send to

Choose Destination
Theor Appl Genet. 1989 Sep;78(3):305-10. doi: 10.1007/BF00265288.

Mutants for rice storage proteins : 2. Isolation and characterization of protein bodies from rice mutants.

Author information

Research Institute for Food Science, Kyoto University, Uji, 611, Kyoto, Japan.


Rice storage proteins of the endosperm are localized in two types of protein bodies, PB-I and PB-II. Protein bodies were isolated by sucrose density gradient centrifugation from developing endosperm of three rice mutants, CM 21, CM 1675 and CM 1834, and characterized after pepsin-digestion treatment by protein contents determination. Mutant protein bodies (PBs) except for their internal structure, were similar in shape and density to PB-I of the variety Kinmaze. Electrophoretic analysis of PB-I polypeptides revealed that SDS (Sodium dodecylsulfate) bands of 13 and 16 kilodaltons consisted, respectively, of four and two individual polypeptides with different pI values, while the 10-kilodalton band behaved as a single polypeptide after isoelectric focussing (IEF) electrophoresis. The differences in the polypeptide composition induced by mutants were due to the decrease and/or increase in the content of specific PB-I polypeptides. Electron microscopic observations revealed that the typical lamellar structure of the PB-I is not visible in CM 1675. On the contrary, the inner portion of PB-I in CM 1834 and CM 21 showed higher electron density than that of the variety Kinmaze. On these two mutants, the content of pepsin-indigestible and -digestible proteins were similar to those of Kinmaze, although the values of the PB-II/PB-I ratio were greater than those for Kinmaze, suggesting that these two mutants are high-glutelin rice mutants.


Supplemental Content

Loading ...
Support Center