S-carboxymethylated (SCM) matrix proteins from fifteen normal human scalp hair specimens were analyzed using two-dimensional polyacrylamide gel electrophoresis (PAGE) with usual isoelectric focusing electrophoresis as the first dimension and then with usual sodium dodecyl sulfate-PAGE as the second dimension. On the electrophoregrams obtained, one low-mobility smear of SCM proteins embedding one SCM protein band was always seen. Many higher-mobility SCM protein spots were also always seen. However, some variations were seen in these SCM protein compositions; in type I, there were eighteen SCM protein components and, in type II, seventeen components.