Elongation factor G (EF‐Gchl) and elongation factor Tu (EF‐Tuchl) have been purified from isolated spinach chloroplasts. On polyacrylamide gel electrophoresis the purified proteins appear to be at least 70% pure. The molecular weight has been estimated to be 77000 and 45500 for EF‐Gchl and EF‐Tuchl respectively.Chloroplast eiongation factor T (EF‐Tchl) has been only partially purified. Gel electrophoresis under non‐denturing and denaturing conditions indicate that EF‐Tchl is most probably composed of two polypeptides, one of which has an electrophoretic mobility identical to that of EF‐Tuchl.EF‐Tuchl appears to represent approximately 7% of the chloroplast soluble protein while EF‐Gchl accounts for less than 1%. Just as in the case of the bacterial factors, EF‐Tuchl appears to be in excess as compared to EF‐Gchl.Although no data were obtained on the concentration of EF‐Tchl, it may be assumed that the three elongation factors represent approximately 10% of the chloroplast soluble protein.