ABSTRACT
Background: Pterygium is a triangular wing shaped fiovascular growth of subconjunctival tissue on to the cornea. Surgical removal is the treatment of choice but no single technique is successful due to high recurrence rate. Aim: To evaluate the success and complications of sutureless glue–free conjunctival–limbal autografting in management of primary pterygium. Materials and Methods: A prospective interventional study was carried out in 60 patients to analyse the outcome of sutureless and glue–free conjunctival–limbal autograft for the management of primary nasal pterygium. The patients were followed up after 1 week, 3 weeks, 6 weeks and at 3 months postoperatively. The mean age of the patients was 38.28± 13.77 years (range 21–67), 55% of which were females. Graft retraction occurred in 3(5%) eyes. Haemorrhage was seen in 20(33.33%) eyes at 24 hours, which persisted in only 8(13.33%) eyes at 3 weeks and resolved completely in 100% of eyes at 6 weeks. Oedema was noted in 5(8.33%) eyes at 24 hours, and resolved completely by 1 week. Recurrence of pterygium was observed in 2(3.33%) eyes at three months of follow–up. Conclusion: Sutureless and glue–free conjunctival–limbal autograft following pterygium excision is an easy, quick, safe, effective, and economical option for the management of primary pterygium.
ABSTRACT
The canine Parvovirus 2, non-structural 1(NS1) is a novel candidate tumor suppressor gene. To confirm the expression of the NS1 in HeLa cells after transfection there was a need to raise antiserum against CPV2- NS1. Therefore, this study was carried out to express and purify the recombinant NS1(rNS1), and characterize the polyclonal serum. CPV2-NS1, complete coding sequence (CDS) was amplified, cloned in pET32a+ and expressed in BL21 (DE3) (pLysS). SDS–PAGE analysis revealed that the expression of the recombinant protein was maximum when induced with 1.5 mM IPTG. The 6 × His tagged fusion protein was purified on Ni-NTA resin under denaturing conditions and confirmed by western blot using CPV2 specific antiserum. The rabbits were immunized with the purified rNS1 to raise anti-NS1 polyclonal antiserum. The polyclonal serum was tested for specificity and used for confirming the expression of NS1 in HeLa transfected with pcDNA.cpv2.ns1 by indirect fluorescent antibody test (IFAT), flow cytometry and western blot. The polyclonal antiserum against NS1 could be very useful to establish functional in vitro assays to explore role of NS1 in cancer therapeutics.