This book is the 2^nd improved and expanded edition of 'Clinical Enzymology' (Lott/Wolf, 1987). It includes case studies and guidelines for specialists of laboratory medicine and clinicians, devotes each chapter to a specific enzyme or protein marker, contains case studies and guidelines, a section on marker biochemistry and physiology as well as a section on special pathology and analysis. The clear, didactic structure and the multiple choice questions also make the book valuable reading for graduate students in the fields of clinical pathology and laboratory medicine.

Steven C. Kazmierczak, Health & Science University, Portland, Oregon, USA; Hassan M. E. Azzazy, American University in Cairo, Egypt.

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