Alekseeva A E, Grebenshchikova O G, Potapkina T A, Prozorovskiĭ V N
Vopr Med Khim. 1989 Jul-Aug;35(4):66-72.
N-terminal peptide was isolated from BrCN hydrolysate of pig muscle lactate dehydrogenase (LDH), its antigenic properties were studied using solid-phase immunoenzyme assay. N-terminal fragment containing 1-32 amino acids of LDH exhibited the antigenic activity towards antiserum and specific antibodies to native LDH5 and inhibited formation of the antigen-antibody complex by 25-35%, thus suggesting the presence of at least one antigenic determinant in the N-terminal fragment. The N-terminal peptide of LDH5 conjugated with bovine albumin maintained the antigenic activity towards specific antibodies against native LDH5 (inhibition by 20-25%).
从猪肌肉乳酸脱氢酶（LDH）的溴化氰水解产物中分离出N端肽段，采用固相免疫酶测定法研究其抗原特性。含有LDH 1 - 32个氨基酸的N端片段对天然LDH5的抗血清和特异性抗体表现出抗原活性，并使抗原-抗体复合物的形成受到25% - 35%的抑制，这表明N端片段中至少存在一个抗原决定簇。与牛血清白蛋白偶联的LDH5的N端肽段对针对天然LDH5的特异性抗体仍保持抗原活性（抑制率为20% - 25%）。
