Granstrom D, Swamy M, Abraham E, Takemoto L
Division of Biology, Kansas State University, Manhattan 66506.
Curr Eye Res. 1989 Jun;8(6):589-93. doi: 10.3109/02713688908995758.
Antisera to synthetic peptides corresponding to residues 229-237, 252-259, and 256-263 have been used to quantitatively bind to the 19.5K, 24.0K, and 26.5K forms of the Major Intrinsic Polypeptide (MIP26K) of lens membrane from the streptozotocin-induced diabetic rat. The binding ratio of anti-229/anti-252 for the 19.5K component, and the binding ratio of anti-252/anti-256 for the 26.5K component, both increase only during the opacification process of the diabetic lens. Together, these results demonstrate that various forms of the MIP26K molecule undergo covalent modification during cataractogenesis of the diabetic rat lens, and that the degree of this change as monitored by binding of the anti-MIP26K peptide sera correlates with severity of the lens opacification.
针对与229 - 237、252 - 259和256 - 263位残基相对应的合成肽的抗血清，已被用于与链脲佐菌素诱导的糖尿病大鼠晶状体膜的主要内在多肽（MIP26K）的19.5K、24.0K和26.5K形式进行定量结合。19.5K组分的抗229/抗252结合比，以及26.5K组分的抗252/抗256结合比，均仅在糖尿病晶状体的浑浊化过程中增加。这些结果共同表明，在糖尿病大鼠晶状体的白内障形成过程中，MIP26K分子的各种形式发生了共价修饰，并且通过抗MIP26K肽血清的结合监测到的这种变化程度与晶状体浑浊的严重程度相关。
