쥐노래미(Hexagrammos otakii) 눈 조직의 젖산탈수소효소(EC 1.1.1.27, lactate dehydrogenase, LDH) eye-specific C_4 동위효소를 affinity chromatography 및 continuous-elution electrophoresis system으로 정제하였다. 정제된 eye-specific LDH C_4 동위효소의 분자량은 154.8 kDa이었다. 효소반응의 최적 pH는 8.5로 나타났다. 피루브산을 기질로 하였을 때 eye-specific LDH C_4 동위효소의 Km^PYR 값은 1.88×10^-5 M로 나타났다. 본 실험결과 eye-specific LDH C_4 동위효소의 활성 측정 시 pH를 고려해야만 하고 eye-specific LDH C_4 동위효소는 LDH A_4 동위효소보다 피루브산에 대한 기질결합친화성이 큰 것으로 나타났다. 생성된 eye-specific LDH C_4 동위효소에 대한 항체는 사람에서의 병증진단 및 어류에서의 비교생리학적 연구에 폭 넓게 사용될 것이라고 생각된다.Eye-specific lactate dehydrogenase (EC 1.1.1.27, LDH) C_4 isozyme in the eyes of greenlings (Hexagrammos otakii) was successfully purified by affinity chromatography and continuous-elution electrophoresis. The molecular weight of the purified eye-specific LDH C_4 isozyme was 154.8 kDa, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimal pH for enzymatic reaction of the eye-specific LDH C_4 isozyme was pH 8.5. Km^PYR value of the purified eye-specific LDH C_4 isozyme was 1.88×10^-5 M using pyruvate as a substrate. These results indicate that we must consider pH when measuring eye-specific LDH C_4 isozyme activity. The eye-specific LDH C_4 isozyme had a higher binding affinity for the substrate as a pyruvate than LDH A_4 isozyme. Antibodies produced against the purified eye-specific LDH C_4 isozyme may be used in the diagnosis of several human diseases and in comparative physiological studies of fishes.