ABSTRACT
AIM:To study the changes of tear film and ocular surface after the coaxial micro incision 2. 2mm and 2. 8mm in the phacoemulsification. METHODS:Eighty-six patients ( One hundred and six eyes ) from 2014/06 to 2016/01 in our hospital were enrolled. The patients were randomly divided into two groups. Forty-four patients ( Fifty-three eyes) in group A: coaxial 2. 2mm micro- incision phacoemulsification cataract extraction and intraocular lens(IOL) implantation;Forty-two patients ( Fifty-three eyes ) in group B: the conventional coaxial 2. 8mm small incision phacoemulsification cataract extraction and IOL implantation. The break up time ( BUT) , dry eye symptom ( DES) score, Schirmer's I test ( SⅠt ) and lid-wiper epitheliopathy ( LWE ) score were assessed preoperatively and postoperatively. RESULTS:At 1wk, 1 and 2mo postoperatively, the BUT in two groups decreased after operations, and the BUT of group B was significantly lower than those of group A, the differences were statistically significant ( t = 3. 098, 4.512, 4.329; all P 0. 05). The BUT, DES score, SⅠt and LWE score in group B showed statistically significant differences (t=-4. 063, 7. 306, 3. 621, 4. 208;all P<0. 05).CONCLUSION:Ocular surface has less damage and tear film has little influence at early stage after the coaxial 2.2mm microincision phacoemulsification, compared with the conventional coaxial 2. 8mm incision phacoemulsification surgery.
ABSTRACT
<p><b>OBJECTIVE</b>To provide materials for the study of the function of ESC42 protein specifically expressed in the human epididymis.</p><p><b>METHODS</b>The ESC42 gene was amplified from the human epididymis cDNA library by PCR and then cloned into prokaryotic expression vector pGEX-4T-1, expressed and purified by recombinant DNA techniques. The specificity of ESC42 protein was identified by Western blot and MALDI-TOF-MS. The database was searched by Ms-Fit.</p><p><b>RESULTS</b>The recombinant plasmid expressed a Mr 38 x 10(3) fusion protein in E. coli at a level of 30% of the total protein, and the purity was as high as 99%. The ESC42 protein was identified by ESC42 monoclonal antibody and its molecular weight was 11 978.12, tested by MALDI-TOF-MS. The peptide mass fingerprint analysis showed that the coverage rate of the sequence reached 48% with 100% matching. The motif scan in Prosite database reveal that ESC42 belonged to the beta-defensin family and had antibacterial activity.</p><p><b>CONCLUSION</b>Obtaining high purity of rhESC42 protein may lay a foundation for the study of its functions.</p>