An immunological comparison of several novel calcium-binding proteins.
Polyclonal antibodies prepared against each of the calcimedins were utilized to determine their tissue distribution. The immunological survey of rat tissues revealed that the levels of the 35-kDa calcimedin varied, while the amount of the 67-kDa calcimedin was relatively constant in the tissues examined. A new immunoreactive species, 52 kDa, was detected with the antibody to the 35-kDa calcimedin; this protein appears to be the predominant immunoreactive species in the tissues examined. Antibodies to the 35-kDa calcimedin were also used to compare many other calcium-binding proteins in order to determine immunological relationships. These comparisons demonstrate that the epidermal growth factor receptor/kinase substrate (p35), the src kinase substrate (pp36), and calregulin are immunologically unrelated to the calcimedins. However, it was found that the 67-kDa calcimedin and the p70 calelectrin are identical, as are the 35-kDa calcimedin and the p32.5 calelectrin. The calimedins are a subset of the chromobindins. In addition, the antibody to the 35-kDa calcimedin also cross-reacts with synexin, which may be related to the new 52-kDa immunoreactive protein identified.
D000595:Amino Acid Sequence; D000818:Animals; D017302:Annexins; D000906:Antibodies / Q000276:immunology; D002135:Calcium-Binding Proteins / Q000032:analysis / Q000276:immunology* / Q000502:physiology; D037282:Calreticulin; D003429:Cross Reactions; D051381:Rats; D012261:Ribonucleoproteins / Q000032:analysis / Q000276:immunology* / Q000502:physiology
D017302:Annexins; D000906:Antibodies; D002135:Calcium-Binding Proteins; D037282:Calreticulin; D012261:Ribonucleoproteins