Abstract
Four electrophoretic variants of acid phosphatase have been already reported in the silkworm hemolymph. We found an electrophoretic variant (type E) which had been designated O (null) type since the distinct band had not been detected. The band E was undiscernible when the substrate (α-Naphthyl phosphate) and chromogen (Fast blue B) were poured simultaneously on the gel after electrophoresis according to the former procedure. However, if the gel was incubated with α-NP then Fast blue B was added, a distinct band E appeared. Quantitative analyses showed that Fast blue B inhibited the isozyme E competitively but other isozymes noncompetitively. Several lines of experimental evidence suggest the isozyme E is not only a charge isomer but also an isozyme showing different kinetic properties with other isozymes. By crossing experiments isozymes A-E were considered to be controlled by codominant alleles, BphA-BphE, respectively.
