Sharief F S, Wilson S H, Li S S
Biochem J. 1986 Feb 1;233(3):913-6. doi: 10.1042/bj2330913.
A 36,000-Mr protein purified from mouse myeloma on the basis of selective binding to a single-stranded DNA (ssDNA)-cellulose column has been identified as the lactate dehydrogenase A (LDH-A) subunit. A homogeneous preparation of this mouse myeloma ssDNA-binding protein, termed the 'low-salt-eluting protein', was found to possess LDH activity, and rabbit antiserum prepared against this protein was shown to cross-react with purified 36,000-Mr LDH-A subunits from mouse and bovine sources. In addition, bovine and human LHD-A4 isoenzymes were shown to be capable of binding ssDNA. These enzymic and immunological identities with LDH-A were not observed with purified helix-destabilizing protein 1 from mouse myeloma. A model for ssDNA-LDH binding is discussed.
从鼠骨髓瘤中通过与单链DNA（ssDNA）-纤维素柱的选择性结合而纯化得到的一种36000道尔顿的蛋白质，已被鉴定为乳酸脱氢酶A（LDH-A）亚基。这种鼠骨髓瘤ssDNA结合蛋白的纯化物，被称为“低盐洗脱蛋白”，被发现具有LDH活性，并且针对该蛋白制备的兔抗血清被证明能与从小鼠和牛源纯化得到的36000道尔顿的LDH-A亚基发生交叉反应。此外，牛和人的LHD-A4同工酶被证明能够结合ssDNA。从小鼠骨髓瘤中纯化得到的螺旋去稳定蛋白1则未观察到这些与LDH-A的酶学和免疫学一致性。文中讨论了ssDNA-LDH结合的模型。
