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1.
Article in Chinese | WPRIM | ID: wpr-679016

ABSTRACT

Objective To explore the effects of survivin on radiation injury and its relation to caspase 9/6,3 activity. Methods ① IEC 6 cells were treated under hypoxic environment for 8 h and followed by reoxygenation for 24 and 48 h, and then the expression of survivin was identified by Western blotting. ② After treatment with 35 Gy 60 Co , the apoptosis rate in different groups was detected with FACS and the caspase 9/6,3 activity was tested using the caspase 9/6,3 assay kit. Results Hypoxic preconditioning could induce the expression of survivin in IEC 6 cells and survivin could decrease the caspase 3 activity, resulting in reduced apoptosis rate induced by radiation. Conclusion Survivin induced by hypoxic preconditioning can inhibit the apoptosis induced by radiation by reducing the caspase 3 activity.

2.
Article in Chinese | WPRIM | ID: wpr-556334

ABSTRACT

Objective To observe the expressions of C/EBPs mRNA and protein in the sebaceous gland and to study the relationship between C/EBPs and the differentiation of sebocytes. Methods RT-PCR and immunhischemistry were used to detect the expressions of C/EBPs mRNA and protein in the embryo and adult sebaceous glands. Results The lowest expression of C/EBP? mRNA in the sebaceous gland was found in embryonic period, but increased gradually during the developmental stages. The expression of C/EBP? mRNA in the sebaceous gland showed different expression patterns, i.e. it maintained at low level in all of the developmental stages. Expressions of C/EBP? and ? protein were found in the nuclei of sebocytes in embryonic period but in the basal cell layer of sebaceous glands in maturation phase. Conclusion The expression patterns of C/EBPs are different in the sebaceous gland from embryonic to adult stages, suggesting that C/EBP? and ? may play important roles in the development of human sebaceous gland.

3.
Article in Chinese | WPRIM | ID: wpr-519667

ABSTRACT

AIM: To purify and refold the inclusion body of a human anti-HBsAg scFv with a 6?His tag, and to determine the affinity constant of the purified recombinant product.METHODS: Solubilizing in buffers containing urea or guanidine hydrochloride (GuHCl), the inclusion body was purified by IMAC, and then refolded by dialysis against urea or GuHCl, at the same time, Ni 2+ charged chelate column was utilized for in situ refolding. The affinity constant of the refolded scFv, polished by immune-affinity chromatography, was determined by non-competitive ELISA. RESULTS: The refolded scFv with highest specific bioactivity was produced by dialysis against GuHCl. Under this condition, the recovery of target protein reached (61.08?1 45)%. The affinity constant of the polished scFv was confirmed to be(2.30?0.32) ?10 7 L/mol. CONCLUSION: The inclusion body studied in this paper can be refolded efficiently under optimal dialysis condition in vitro . The antigen-binding property of this recombinant scFv is not affected by the purification tag fused to the N terminal of the protein.

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