MATERIALS AND METHODS: To determine the extent of variation in reporting of protein electrophoresis results questionnaires were distributed to the pathologists of various laboratories in Malaysia regarding the method, quantification of paraprotein concentrations and immunoglobulin assays, and information regarding current laboratory electrophoresis practices.
RESULTS: Variation was found in the following reporting practices: (a) screening protocol; (b) reporting of serum albumin; (c) numerical reporting of protein fractions and paraprotein; (d) co-migration of a paraprotein with a normal serum protein; (e) reporting of multiple paraprotein bands (f) appearance of small abnormal band and oligoclonal bands and (g) communication about of interferences.
CONCLUSION: The pathologists of the country made recommendations on the reporting of protein electrophoresis. Harmonised reporting will reduce inconsistency, variation in reporting, improve the quality of the report and most importantly improve patient care.
METHODS: The PkDBPαII of Peninsular Malaysia and Malaysian Borneo were expressed on the surface of COS-7 cells and tested with human and monkey erythrocytes, with and without anti-Fy6 (anti-Duffy) monoclonal antibody treatment. Binding activity level was determined by counting the number of rosettes formed between the transfected COS-7 cells and the erythrocytes.
RESULTS: Anti-Fy6 treatment was shown to completely block the binding of human erythrocytes with the transfected COS-7 cells, thus verifying the specific binding of human DARC with PkDBPαII. Interestingly, the PkDBPαII of Peninsular Malaysia displayed a higher binding activity with human erythrocytes when compared with the Malaysian Borneo PkDBPαII haplotype (mean number of rosettes formed = 156.89 ± 6.62 and 46.00 ± 3.57, respectively; P
METHODS AND RESULTS: Ten naturally occurring phenolic compounds were assessed for their inhibitory effect on the hydrolytic enzymes of G. boninense. The enzyme kinetics (Vmax and Km ) and the stability of the hydrolytic enzymes were also characterized. The selected compounds had shown inhibitory effect at various concentrations. Two types of inhibitions namely uncompetitive and noncompetitive were observed in the presence of phenolic compounds. Among all the phenolic compounds tested, benzoic acid was the most effective compound suppressive to the growth and production of hydrolytic enzymes secreted by G. boninense. The phenolic compounds as inhibitory agents can be a better replacement for the metal ions which are known as conventional inhibitors till date. The three hydrolytic enzymes were stable in a wide range of pH and temperature.
CONCLUSION: These findings highlight the efficacy of the applications of phenolic compounds to control Ganoderma.
SIGNIFICANCE AND IMPACT OF THE STUDY: The study has proved a replacement for chemical controls of G. boninense with naturally occurring phenolic compounds.