Total RNA, polyribosomes and polyribosomal RNA have been isolated from immature wheat grain and used to prime the wheat-germ cell-free protein synthesis system to produce storage protein. The synthesis of wheat prolamins, a major fraction of storage proteins, was mainly associated with membrane-bound polyribosomes. The ratio of bound to free polyribosomes increased from one at 8 days to approximately three at 32 days post-anthesis. SDS polyacrylamide gel electrophoresis and fluorography of the prolamins showed that the same components were being synthesized and accumulated from 12 days post-anthesis onward. Evidence is presented that prolamins within the molecular weight range 35 000-45 000 may be translated with a signal sequence attached. These signal sequences are rapidly removed during translation and further post-translational modifications may occur over longer periods.

A potential application of plant proteins could be a replacement of animal proteins now in use in the food industry on the basis of certain specific functional properties plant proteins have. Modification of the chemical structure of selected plant proteins is needed to replace more expensive animal proteins as food ingredients that have specific functional characteristics. Structure modification may be achieved by physical, chemical, or microbiological methods, or by a combination of these. Immobilized enzyme techniques offer significant advantages for protein modification. Knowledge of the molecular properties of plant proteins is essential to understand the basis of protein functionality, to modify proteins so that they acquire desirable functional properties, and to predict potential applications of modified plant proteins. This paper reviews all the above mentioned aspects of plant protein chemistry and potential utilization.