Xie Zhou;Jin, Zhen-hua;Zheng, Zhi-fu;Kai Xia;Zhang, Neng-gang;Wan, Yin-sheng;Sang, Yong-ming;Chen, Kao-shan;Liu, Shi-ming
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Two types of immunoloigcal probes, anti-ABBP Abs, have been developed. The purified ABBP from ABA-C1-BSA-sepharose 4B column was identified by PAGE and appeared in one band of about 56KD, as well as showed a specific binding ability and a high affinity for ABA (Kd2.0$\times$10-9 mol/L). Unexpectedly, the existence of rRNA with a length of around 300 nucleotides could be found, when the ABBP was digested with proteinase K and identified by eletrophorsis on an agarose gel (1%). As a result, about 120 cDNA clones coding maize 17s RNA and only one cDNA clone coding ABBP (24cDNA) were obtained from 200,000 seperated phage plaques by the anti-ABBP pAbs. 24cDNA had 1075bp and contained an open reading frame coding 254 amino acids. The anti-idiotypic Ab raised against an ABA MAb showed the ability of either mimicking ABA or competing with ABA. The localization of ABBPs in plant cell was investigated.