A clinical audit was conducted for a 4-year period at the Universiti Kebangsaan Malaysia (UKM) Ophthalmology Department in which 61 eyes of adult patients with primary glaucoma underwent trabeculectomies without antimetabolites. At a 2-year follow-up duration, successful trabeculectomies as defined by intraocular pressure below 20 mm Hg without additional glaucoma medication were 62% for primary open-angle glaucoma, 48% for primary acute angle-closure glaucoma and 43% for chronic angle-closure glaucoma. 50.8% of eyes were without complications while 49.2% had complications. Shallow anterior chamber (22.9%) and hyphaema (19.7%) were the two commonest complications.
This study was a retrospective study on corneal ulcer of one year period in Hospital Ipoh. A total of 28 cases were studied. Among the risk factors identified were foreign body on cornea, trauma, contact lens, vernal keratoconjunctivitis and surgical complication. The nature of this disease which was severe and slow healing caused prolonged hospital admission. Identification of causative microorganism by corneal scraping help in the treatment and management of this condition.
GDSL esterase is designated as a member of Family II of lipolytic enzymes known to catalyse the synthesis and hydrolysis of ester bonds. The enzyme possesses a highly conserved motif Ser-Gly-Asn-His in the four conserved blocks I, II, III and V respectively. The enzyme characteristics, such as region-, chemo-, and enantioselectivity, help in resolving the racemic mixture of single-isomer chiral drugs. Recently, crystal structure of GDSL esterase from Photobacterium J15 has been reported (PDB ID: 5XTU) but not in complex with substrate. Therefore, GDSL in complex with substrate could provide insights into the binding mode of substrate towards inactive form of GDSL esterase (S12A) and identify the hot spot residues for the designing of a better binding pocket. Insight into molecular mechanisms is limited due to the lack of crystal structure of GDSL esterase-substrate complex. In this paper, the crystallization of mutant GDSL esterase (S12A) (PDB ID: 8HWO) and its complex with butyric acid (PDB ID: 8HWP) are reported. The optimized structure would be vital in determining hot spot residue for GDSL esterase. This preliminary study provides an understanding of the interactions between enzymes and hydrolysed p-nitro-phenyl butyrate. The information could guide in the rational design of GDSL esterase in overcoming the medical limitations associated with racemic mixture.