Actin and myosin solutions and fresh ground pork were irradiated with the electron beam (e-beam) at a dose of 0, 1.5, 3.0, 5.0 and 10 kGy. The changes in SDS-PAGE pattern of 2 proteins and the salt-soluble proteins extracted from ground pork after e-beam irradiation were monitored. When the myosin solution was irradiated with e-beam, myosin was degraded completely. Complete myosin degradations were observed even with the lowest dose (1.5 kGy) of e-beam treatment. Actin was degraded with the irradiation, but to a less extent than myosin was. The degradation of actin increased as the e-beam treatment increased from 1.5 to 10.0 kGy. Among the salt-soluble proteins extracted from ground pork, myosin was degraded gradually when the e-beam dose increased from 1.5 up to 10.0 kGy. Similar gradual increase in the degradation of actin also occurred with the increase of irradiation. Increases of 2 low molecular weight compounds (<29 kDa) were observed when the irradiation dose increased from 1.5 to 10.0 kGy. These 2 molecules are thought to be the breakdown products produced from the degradation of major salt-soluble proteins, myosin and actin. The salt-soluble protein content of ground pork did not change with the e-beam irradiation.