BINDING PROPERTIES OF BOVINE OCULAR LENS ZETA-CRYSTALLIN TO RIGHT-HANDED B-DNA, LEFT-HANDED Z-DNA, AND SINGLE-STRANDED DNA

摘要: Abstract Bovine zeta-crystallin has the ability to bind with different DNAs. Initially, this protein was named regulatory factor 36 (Kang et al. , 1985), but it been shown be an ocular lens (Jornvall 1993), which is considered enzyme-crystallin (Rodakanaki 1989). The enzyme-linked immunosorbent assay (ELISA) used quantitate binding of bovine purified high molecular weight double-stranded (ds-) and single-stranded (ss-) DNA (bovine synthetic DNA). ELISA quantitation achieved by addition anti-zeta-crystallin antibodies DNA–zeta-crystallin complex, using a novel immunochemical avidin–biotin method. Zeta-crystallin shows much greater intensity for ss-DNA ds-Z-DNA than ds-B-DNA. It also reacts slightly more ss-DNA. Therefore, we speculate that may act as transcriptional enhancer (outer cortex), possibly Z-DNA elements within crystallin genes. protect from endogenous DNase activity unwinding (destabilizing) involved transcription, occurring in normal adult nucleated secondary fiber cells.