1;Preface;5 2;List of contributing authors;7 3;1 Angiotensin converting enzyme;17 3.1;1.1 Case studies;17 3.1.1;1.1.1 Patient A;17 3.1.2;1.1.2 Patient B;17 3.1.3;1.1.3 Patient C;18 3.2;1.2 Biochemistry and physiology;19 3.2.1;1.2.1 Physiological function;19 3.2.2;1.2.2 Biochemistry and molecular forms;19 3.2.3;1.2.3 Tissue sources;21 3.2.4;1.2.4 Reference ranges;21 3.3;1.3 Chemical pathology;23 3.3.1;1.3.1 ACE in sarcoidosis;23 3.4;1.4 Analysis;25 3.4.1;1.4.1 Specimen;25 3.4.2;1.4.2 Spectrophotometric methods;26 3.4.3;1.4.3 High-performance liquid chromatography;26 3.4.4;1.4.4 Fluorometric methods;27 3.4.5;1.4.5 Radioassays;27 3.4.6;1.4.6 Other methods;27 3.4.7;1.4.7 Inhibitors of ACE;28 3.5;1.5 Questions and answers;28 4;References;29 5;2 Acetylcholinesterase and butyrylcholinesterase;35 5.1;2.1 Case studies;35 5.1.1;2.1.1 Patient A;35 5.1.2;2.1.2 Patient B;36 5.1.3;2.1.3 Patient C;37 5.1.4;2.1.4 Patient D;38 5.1.5;2.1.5 Patient E;38 5.2;2.2 Biochemistry and physiology of the cholinesterases;39 5.2.1;2.2.1 Molecular forms;39 5.2.2;2.2.2 Inheritance of BChE variants;42 5.3;2.3 Chemical pathology;45 5.3.1;2.3.1 Pesticide and nerve agent poisoning;45 5.4;2.4 Analytical measurements of AChE and BChE;52 5.4.1;2.4.1 Desired specimens;52 5.5;2.5 Questions and answers;54 6;References;56 7;3 Aldolase;57 7.1;3.1 Case studies;57 7.1.1;3.1.1 Patient A;57 7.1.2;3.1.2 Patient B;58 7.1.3;3.1.3 Patient C;59 7.2;3.2 Biochemistry and physiology;59 7.2.1;3.2.1 Physiological function;59 7.2.2;3.2.2 Biochemistry and molecular structure;60 7.2.3;3.2.3 Tissue source(s) and expression of ALD;61 7.2.4;3.2.4 Clearance and metabolism of ALD;61 7.2.5;3.2.5 Reference ranges;62 7.3;3.3 Chemical pathology;63 7.3.1;3.3.1 Polymyositis/dermatomyositis;63 7.3.2;3.3.2 Duchenne muscular dystrophy;64 7.3.3;3.3.3 Drug-induced myopathy;64 7.3.4;3.3.4 Pathologies in which CK does not reflect the extent of muscle damage;65 7.4;3.4 Analysis;66 7.4.1;3.4.1 Specimen;66 7.4.2;3.4.2 Analyte stability;67 7.4.3;3.4.3 Interferences;67 7.4.4;3.4.4 Reference methods;67 7.5;3.5 Questions and answers;68 8;References;69 9;4 Alkaline phosphatase;73 9.1;4.1 Case studies;73 9.1.1;4.1.1 Patient A;73 9.1.2;4.1.2 Patient B;74 9.1.3;4.1.3 Patient C;75 9.1.4;4.1.4 Patient D;76 9.1.5;4.1.5 Patient E;76 9.1.6;4.1.6 Patient F;77 9.2;4.2 Biochemistry and physiology;79 9.2.1;4.2.1 Structure;79 9.2.2;4.2.2 Physiological function of ALP in tissue/blood/other fluids;82 9.2.3;4.2.3 Tissue sources of ALP;82 9.2.4;4.2.4 Clearance/metabolism of enzyme;83 9.2.5;4.2.5 Reference ranges;83 9.3;4.3 Chemical pathology;84 9.3.1;4.3.1 Liver disease;84 9.3.2;4.3.2 Bone disease;85 9.3.3;4.3.3 Metastatic cancer;85 9.3.4;4.3.4 Miscellaneous pancreatic disorders;85 9.3.5;4.3.5 Cystic fibrosis;86 9.3.6;4.3.6 Chronic renal failure;86 9.3.7;4.3.7 Drug therapy;86 9.3.8;4.3.8 Miscellaneous;87 9.4;4.4 Analysis;87 9.4.1;4.4.1 Technical problems;87 9.4.2;4.4.2 Reference method;88 9.4.3;4.4.3 Isoenzyme analysis;88 9.5;4.5 Questions and answers;91 10;Acknowledgements;91 11;References;92 12;5 Aspartate aminotransferase and alanine aminotransferase;97 12.1;5.1 Case studies;97 12.1.1;5.1.1 Patient A;97 12.1.2;5.1.2 Patient B;98 12.1.3;5.1.3 Patient C;98 12.1.4;5.1.4 Patient D;99 12.1.5;5.1.5 Patient E;100 12.2;5.2 Biochemistry and physiology;100 12.2.1;5.2.1 Molecular forms;100 12.2.2;5.2.2 Biochemical function;102 12.2.3;5.2.3 Normal physiology;102 12.2.4;5.2.4 Reference ranges;104 12.3;5.3 Chemical pathology;105 12.3.1;5.3.1 Liver disease;105 12.3.2;5.3.2 Hemochromatosis;108 12.3.3;5.3.3 Skeletal muscle disease;109 12.3.4;5.3.4 Heart disease;110 12.3.5;5.3.5 Other causes of AST increase;111 12.4;5.4 Analysis;111 12.4.1;5.4.1 Specimens;111 12.4.2;5.4.2 Reaction used;111 12.4.3;5.4.3 Interferences;112 12.4.4;5.4.4 Methods for AST isoenzymes;113 12.5;5.5 Questions and answers;113 13;References;114 14;6 Creatine kinase, isoenzymes, and isoforms;121 14.1;6.1 Case studies;121 14.1.1;6.1.1 Patient A;121 14.1.2;6.1.2 Patient B;122