Cell-free translation systems can synthesize proteins with high accuracy and speed approaching in vivo rates [1], and they can express proteins that seriously interfere with cell physiology. In general, however, they are unstable and thus inefficient [2]. Spirin et al. [3] proposed a continuous-flow cell-free (CFCF) translation method, in which a solution containing amino acids and energy sources is supplied to the translation chamber through a semipermeable membrane. In fact, an E. coli cell-free system operated in the CFCF mode gives much higher productivity than a conventional batch system [3]. This system, however, still has inherent limitation because of its prokaryotic nature of translation and folding mechanisms; multidomain proteins, found more often in eukaryotes than in prokaryotes, tend to missfold in prokaryotic systems, whether in vivo or in vitro [4]. Thus, it seems to be a big challenge to improve prokaryotic cell-free systems for the preparation of multidomain proteins. On the other hand, the rabbit reticulocyte cell-free system, a popular system derived from eukaryotic animal cells, cannot be adopted for the synthesis of preparative amounts of proteins because of its low efficiency and a high endogenous globin content which obstructs product purification. One of the most convenient and promising eukaryotic cell-free translation systems is conceivably the one based on wheat embryos in which all the components of translation are stored in a dried state, ready for protein synthesis as soon as germination starts. Derived from a eukaryotic plant source, it is expected to have the ability to synthesize eukaryotic multidomain proteins in the folded state. The conventional wheat germ system, however, is plagued with its short life; as a result, it is as inefficient as other cell-free systems.

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