Semantic priming effects (behavioral and electrophysiological) were compared in the visual and auditory modalities across three stimulus onset asynchronies (SOAs; 0, 200, and 800 ms). When both prime and target were presented in the visual modality (the prime just to the left of a fixation point and the target to the right) there were N400 priming effects present across the three SOAs. However, the N400 in the 0-ms SOA condition extended longer in time (800 vs. 500 ms) than in the other SOAs. When both the prime and target were presented in the auditory modality (the prime to the right ear and the target to the left), the largest priming effects were found for the 800-ms SOA. Moreover, there was a relatively early priming effect present in the 0- and 800-ms SOA conditions but not in the 200-ms condition. The results are discussed in terms of modality differences in the time course of word comprehension processes. 相似文献
Anti-Ro sera immunoprecipitate Ro ribonucleoproteins (RNPs) from human cell extracts. Ro RNPs are biochemically heterogeneous particles whose functions are unknown and whose exact composition remains controversial. In addition to 60-kD Ro and to La proteins, a 52-kD polypeptide (p52) has been proposed to be a stable component of the Ro RNPs. To confirm the immunological studies supporting this hypothesis, we have biochemically purified Ro RNPs from HeLa cells using non-denaturing conditions. Ro RNPs segregated into three distinct populations, one of which only contained hY5 RNA (RohY5 RNPs). No p52 co-purified with Ro RNPs. Despite the absence of p52, purified Ro RNPs had biochemical and immunological properties identical to those of unfractionated Ro RNPs. Many anti-Ro sera only recognize p52 in immunoblots, and are said to be monospecific anti-p52. Preincubation with purified RohY5 RNPs (free of p52) of all human anti-Ro (including so-called monospecific anti-p52) sera abolished their capacity to immunoprecipitate Ro RNPs from unfractionated HeLa cell extracts. Conversely, preincubation of anti-Ro sera with purified p52 protein specifically inhibited recognition of p52 in immunoblots, but did not interfere with immunoprecipitation of Ro RNPs. Our data demonstrate that anti-p52 antibodies do not target intact Ro RNPs, nor do they target the native 60-kD Ro protein. Contrary to previous reports, p52 protein is not a stable component of antigenically intact Ro RNPs. 相似文献