Block meat cut from horse mackerel was cured in 3M NaCl (pH 7.5) in the presence and absence of 5 mM EDTA for 3 hr at 4-degrees-C. During drying at 30-degrees-C, changes in the myosin heavy chain and epsilon-(gamma-glutamyl)lysine isopeptide bonds in the meat were observed. After 20 hr drying, cross-linking of the myosin heavy chain was observed and epsilon(gamma-glutamyl)lysine bonds increased eight fold. These changes were inhibited in the presence of EDTA. These results suggested that transglutaminase was probably involved in the cross-linking reaction of the myosin heavy chain in the manufacture of dried fish (''Himono'' in Japan).