Biomedical subjects
Publications and source records attributed to S Apel.
Masling (1998) stated that we did not find the effects of subliminal psychodynamic activation because of experimental artifacts. We reject his assertion that our failure to uncover effects was due to procedural problems and reassert our claim that the method was sound.
18 men and 18 women were tachistoscopically shown the stimuli MOMMY AND I ARE ONE, DADDY AND I ARE ONE, and MYMMO NAD I REA ENO, at subjective thresholds (subliminal condition) and at 500 msec. (supraliminal condition). Following exposure to each stimulus, subjects performed a fine motor line-tracing task. Heart rate was monitored continuously during stimulus presentation and the fine motor task. Analysis showed subjects did not respond more positively with decreased heart rate or fewer errors on the fine motor task following the MOMMY message than the anagram phrase, thereby providing no support for the hypotheses. No correlation was found between responsiveness to the MOMMY message and scores on measures of self-perception and kinship. In the light of mounting negative evidence, the validity of the method of subliminal psychodynamic activation is questioned.
A bile-acid-binding protein of Mr 14000 has been previously identified by photoaffinity labeling in rabbit ileal brush border membrane vesicles [Kramer et al. (1993) J. Biol. Chem. 268, 18035-18046]. This peripheral membrane-associated protein was purified and identified as an ileal lipid-binding protein. It was further shown to be identical to the cytosolic 14-kDa bile-acid-binding protein from the same tissue. Starting with sequence information from tryptic fragments, we cloned and sequenced the gene and its transcript. It has four exons (123, 176, 90, 115 bp) and three introns (1372, 2291, 3137 bp) and a similar structure as the genes from other members of the fatty-acid-binding protein family. The deduced protein has 128 amino acid residues and a calculated molecular mass of 14404 Da. It exhibits high similarity to its human (83%), mouse (77%), rat (76%) and porcine (72%) counterparts. Furthermore, the recombinant protein was produced in Escherichia coli and shown to be identical to native protein from ileal tissue. Functionality of the recombinant protein was demonstrated by labeling with various photoaffinity derivatives of bile acids. Ranking of the photolabeling efficiency of these probes towards the recombinant protein was comparable to the respective ranking towards the native protein. Polyclonal antibodies that were raised in hens against the recombinant protein, specifically recognized the ileal lipid-binding protein in the brush border membrane and cytosol from rabbit ileum. In contrast, no labeling was observed with jejunal tissue. Our results suggest a specific role of the membrane-associated ileal lipid-binding protein for the process of ileal bile acid uptake.