• Korean Journal of Poultry Science
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• v.32 no.1
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• pp.61-66
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• 2005

This experiment was conducted to compare the influences of dietary sea urchin shell powder (SUSP) supplemented to broiler diets on performance, mineral contents and blood cholesterol for 5 weeks. The experimental diets contained 21.5 and $19\%$ CP for the starting and finishing period, respectively The ME was 3,100 kcal/kg of feed in both starter and finisher diets. One hundred sixty chicks were assigned to 4 treatments with 4 replicates and fed one of 4 experimental diets containing different levels of SUSP: 1) Control (commercial feed) 2) T1 (commercial feed with $1\%$ SUSP) 3) T2(commercial feed with $3\%$ SUSP) 4) T3(commercial feed with $5\%$ SUSP). Body weight gain was higher in the T1 group when fed the starter diet (P<0.05), but was the lowest in T1 group for finishing period. Feed efficiency was not significantly different between the control and treatment groups (P>0.05). The total cholesterol of the control was higher than the treatment groups and the HDL-cholesterol were higher in T2 and T3. However, effects of diets containing graded levels of SUSP on LDL-cholesterol and triglyceride contents were not found (P>0.05). The SUSP diets were increased significantly the Fe, Zn and Ca contents of chicken meat, and tended to increase total mineral contents. In conclusion, dietary supplementation of SUSP to broiler diets could be applied to the enhancement of Ca, Fe and total mineral contents levels in chicken meat.

• BMB Reports
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• v.50 no.10
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• pp.485-486
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• 2017

Many intrinsically unstructured/unfolded proteins (IUPs) contain transient local secondary structures even though they are "unstructured" in a tertiary sense. These local secondary structures are named "pre-structured motifs (PreSMos)" and in fact are the specificity determinants for IUP-target binding, i.e., the active sites in IUPs. Using high-resolution NMR we have delineated a PreSMo active site in the intrinsically unfolded mid-domain (residues 201-300) of SUMO-specific protease 4 (SUSP4). This 29-residue motif which we termed a p53 rescue motif can protect p53 from mdm2 quenching by binding to the p53-helix binding pocket in mdm2(3-109). Our work demonstrates that the PreSMo approach is quite effective in providing a structural rationale for interactions of p53-mdm2-SUSP4 and opens a novel avenue for designing mdm2-inhibiting anticancer compounds.