Abstract
The amino acid sequence of the ferredoxin of Triticum aestivum (wheat) was determined by using a Beckman 890C sequencer in combination with the dansyl–phenylisothiocyanate method to characterize peptides obtained by tryptic, chymotryptic and thermolytic digestion of CNBr-cleavage fragments. The molecule consists of a single polypeptide chain of 97 residues and has an unblocked N-terminus. It shows considerable similarity to other plant-type ferredoxins.