Grebenshchikova O G, Prozorovskiĭ V N
Biokhimiia. 1989 Mar;54(3):370-4.
Antipeptide antibodies (AB) to the fragment of the active center of porcine lactate dehydrogenase M4 isoform were used for the analysis of antigenic properties and structural comparison of active centers of human lactate dehydrogenase isoforms. Selective precipitation of the M-subunit-containing isoforms using an immunoadsorbent based on antipeptide AB as well as selective inhibition of the enzymic activity of the M4 isoform by antipeptide AB testify to the specific binding of isoforms to antipeptide AB. The experimental results confirm the literary data on conformational changes in the structure of the active centers of corresponding human lactate dehydrogenase isoforms. The specific interaction of antipeptide AB with human lactate dehydrogenase isoforms suggests that the site of the amino acid sequence (residues 180-214) in both human and porcine M4 isoenzymes is immunochemically identical. The data obtained suggest that antipeptide AB are convenient probes for detecting differences (including minor ones) in the primary and spatial structure of enzymes.
针对猪乳酸脱氢酶M4同工型活性中心片段的抗肽抗体（AB）被用于分析人乳酸脱氢酶同工型的抗原特性及活性中心的结构比较。使用基于抗肽AB的免疫吸附剂对含M亚基的同工型进行选择性沉淀，以及抗肽AB对M4同工型酶活性的选择性抑制，证明了同工型与抗肽AB的特异性结合。实验结果证实了有关相应人乳酸脱氢酶同工型活性中心结构构象变化的文献数据。抗肽AB与人乳酸脱氢酶同工型的特异性相互作用表明，人和猪M4同工酶中氨基酸序列位点（第180 - 214位残基）在免疫化学上是相同的。所获得的数据表明，抗肽AB是检测酶一级结构和空间结构差异（包括微小差异）的便捷探针。
