Arginase Activity as a Useful Cardiac Marker for Differential Diagnosis of UA and MI: A Pilot Study.

Aims: The present study was undertaken to find the levels of aspartate transaminases (AST), creatine kinase (CK-MB) and arginase in serum sample of patients under study and check effectiveness of arginase as a marker in acute coronary syndrome (ACS), and to find the correlation between AST and CK-MB with arginase in unstable angina (UA) and myocardial infarction (MI). Study Design: Case control study carried out at department of Biochemistry, B. J. Medical College Pune, Maharashtra, India, between Sept 2011-Dec 2013. Methodology: The study comprised of clinically diagnosed 60 patients: 30 of UA and 30 of MI. Age and sex matched 30 patients were studied as controls. Blood sample were collected from individual under study, serum was separated and used to estimate levels of CK-MB, AST and arginase. Results: The levels of AST, CK-MB and arginase were estimated and the results were compared with that of control. The levels of arginase were elevated significantly (P<0.001) like AST and CK-MB in patients with MI as compared to UA. In the study there was no correlation observed between CK-MB and arginase in patients of UA or controls. The same was true with the levels of AST and arginase. On the other hand a strong positive correlation was found between CK-MB and AST with arginase in MI patients. Conclusion: It can be concluded that like AST and CK-MB, arginase also increases with progression of ACS. Thus arginase can be used as sensitive marker to differentiate between UA and MI.

Prediction of structure and organisation of chlorophyll a/b binding polypeptides in PS I and II.

Secondary structures, functionally important residues, antigenic sites, membrane spanning segments and hydropathicity of light harvesting chlorophyll a/b binding polypeptides (LHC) are predicted by theoretical methods from the amino acid sequence of the polypeptides. The reported structural features of the Pea LHC (Lhcb 1 gene product) from electron crystallographic studies have been compared by alignment with other types of chlorophyll a/b binding polypeptides for structural prediction. Fifteen conserved residues D85, D89, E113, H116, E/Q133, E/Q181, E189, D/N233, E252, N/H255, Q/E269, E/D/Q280, N281, H285, D288 (number indicates position in the aligned sequence), are identified which are potential ligands to Mg2+ of chlorophylls. Three amino acid residues D89, E/Q131 and D/N 233 are proposed as ligands to chlorophylls b2, a7 and b2 respectively, for which ligands are not identified in electron crystallographic study.