Diagnostic Enzymology (eBook)

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

Preface 5
List of contributing authors 7
1 Angiotensin converting enzyme 17
1.1 Case studies 17
1.1.1 Patient A 17
1.1.2 Patient B 17
1.1.3 Patient C 18
1.2 Biochemistry and physiology 19
1.2.1 Physiological function 19
1.2.2 Biochemistry and molecular forms 19
1.2.3 Tissue sources 21
1.2.4 Reference ranges 21
1.3 Chemical pathology 23
1.3.1 ACE in sarcoidosis 23
1.4 Analysis 25
1.4.1 Specimen 25
1.4.2 Spectrophotometric methods 26
1.4.3 High-performance liquid chromatography 26
1.4.4 Fluorometric methods 27
1.4.5 Radioassays 27
1.4.6 Other methods 27
1.4.7 Inhibitors of ACE 28
1.5 Questions and answers 28
References 29
2 Acetylcholinesterase and butyrylcholinesterase 35
2.1 Case studies 35
2.1.1 Patient A 35
2.1.2 Patient B 36
2.1.3 Patient C 37
2.1.4 Patient D 38
2.1.5 Patient E 38
2.2 Biochemistry and physiology of the cholinesterases 39
2.2.1 Molecular forms 39
2.2.2 Inheritance of BChE variants 42
2.3 Chemical pathology 45
2.3.1 Pesticide and nerve agent poisoning 45
2.4 Analytical measurements of AChE and BChE 52
2.4.1 Desired specimens 52
2.5 Questions and answers 54
References 56
3 Aldolase 57
3.1 Case studies 57
3.1.1 Patient A 57
3.1.2 Patient B 58
3.1.3 Patient C 59
3.2 Biochemistry and physiology 59
3.2.1 Physiological function 59
3.2.2 Biochemistry and molecular structure 60
3.2.3 Tissue source(s) and expression of ALD 61
3.2.4 Clearance and metabolism of ALD 61
3.2.5 Reference ranges 62
3.3 Chemical pathology 63
3.3.1 Polymyositis/dermatomyositis 63
3.3.2 Duchenne muscular dystrophy 64
3.3.3 Drug-induced myopathy 64
3.3.4 Pathologies in which CK does not reflect the extent of muscle damage 65
3.4 Analysis 66
3.4.1 Specimen 66
3.4.2 Analyte stability 67
3.4.3 Interferences 67
3.4.4 Reference methods 67
3.5 Questions and answers 68
References 69
4 Alkaline phosphatase 73
4.1 Case studies 73
4.1.1 Patient A 73
4.1.2 Patient B 74
4.1.3 Patient C 75
4.1.4 Patient D 76
4.1.5 Patient E 76
4.1.6 Patient F 77
4.2 Biochemistry and physiology 79
4.2.1 Structure 79
4.2.2 Physiological function of ALP in tissue/blood/other fluids 82
4.2.3 Tissue sources of ALP 82
4.2.4 Clearance/metabolism of enzyme 83
4.2.5 Reference ranges 83
4.3 Chemical pathology 84
4.3.1 Liver disease 84
4.3.2 Bone disease 85
4.3.3 Metastatic cancer 85
4.3.4 Miscellaneous pancreatic disorders 85
4.3.5 Cystic fibrosis 86
4.3.6 Chronic renal failure 86
4.3.7 Drug therapy 86
4.3.8 Miscellaneous 87
4.4 Analysis 87
4.4.1 Technical problems 87
4.4.2 Reference method 88
4.4.3 Isoenzyme analysis 88
4.5 Questions and answers 91
Acknowledgements 91
References 92
5 Aspartate aminotransferase and alanine aminotransferase 97
5.1 Case studies 97
5.1.1 Patient A 97
5.1.2 Patient B 98
5.1.3 Patient C 98
5.1.4 Patient D 99
5.1.5 Patient E 100
5.2 Biochemistry and physiology 100
5.2.1 Molecular forms 100
5.2.2 Biochemical function 102
5.2.3 Normal physiology 102
5.2.4 Reference ranges 104
5.3 Chemical pathology 105
5.3.1 Liver disease 105
5.3.2 Hemochromatosis 108
5.3.3 Skeletal muscle disease 109
5.3.4 Heart disease 110
5.3.5 Other causes of AST increase 111
5.4 Analysis 111
5.4.1 Specimens 111
5.4.2 Reaction used 111
5.4.3 Interferences 112
5.4.4 Methods for AST isoenzymes 113
5.5 Questions and answers 113
References 114
6 Creatine kinase, isoenzymes, and isoforms 121
6.1 Case studies 121
6.1.1 Patient A 121
6.1.2 Patient B 122
6.1.3 Patient C 123
6.1.4 Patient D 124
6.1.5 Patient E 125
6.2 Biochemistry and physiology 126
6.2.1 Molecular forms 126
6.2.2 CK isoenzymes, atypical forms, and isoforms 127
6.2.3 Reference range 130
6.3 Chemical pathology 130
6.3.1 Heart disease 130
6.3.2 Skeletal muscle disease 132
6.3.3 Trauma 132
6.4 Analytical measurement of total CK and CK-MB 133
6.5 Questions and answers 134
References 135
7 Gamma-glutamyl transferase 137
7.1 Case studies 137
7.1.1 Patient A 137
7.1.2 Patient B 137
7.1.3 Patient C 138
7.1.4 Patient D 139
7.1.5 Patient E 140
7.2 Biochemistry and physiology 140
7.2.1 Molecular forms and post-translational modification 140
7.2.2 Biochemical function 141
7.2.3 Tissue activities and concentrations 141
7.2.4 Metabolic clearance 142
7.2.5 Reference intervals 142
7.3 Chemical pathology 142
7.3.1 Causes of increased or decreased concentrations or activities 142
7.3.2 Diagnostic utility of GGT 143
7.4 Analysis 147
7.4.1 Specimen and stability 147
7.4.2 Preferred method for GGT activity 147
7.5 Questions and answers 148
References 148
8 Lactate dehydrogenase 151
9.1 Case studies 151
8.1.1 Patient A 151
8.1.2 Patient B 152
8.1.3 Patient C 153
8.1.4 Patient D 154
8.1.5 Patient E 155
8.2 Biochemistry and physiology 156
8.2.1 Physiological function 156
8.2.2 Tissue sources 156
8.2.3 Reference ranges 157
8.3 Chemical pathology 157
8.3.1 Cardiology 158
8.3.2 Hepatology 158
8.3.3 Hematology 158
8.3.4 Oncology 159
8.3.5 Neurology 159
8.3.6 Macro-LD 160
8.3.7 Genetic deficiencies 160
8.4 Analysis 160
8.4.1 LD isoenzyme determination 161
8.4.2 IFCC reference method 161
8.4.3 Specimen 162
8.5 Questions and answers 162
References 163
9 Pancreatic lipase 169
9.1 Case studies 169
9.1.1 Patient A 169
9.1.2 Patient B 170
9.1.3 Patient C 171
9.1.4 Patient D 172
9.2 Biochemistry and physiology 173
9.2.1 Molecular forms 173
9.2.2 Molecular structure and tissue expression 174
9.2.3 Mechanism of catalysis 175
9.2.4 Functional regulation 175
9.2.5 Lipase in serum 177
9.2.6 Other lipases 178
9.2.7 Reference range and standardization 180
9.3 Chemical pathology 180
9.3.1 Acute pancreatitis 180
9.3.2 Pancreatic cancer 181
9.3.3 Cystic fibrosis 182
9.3.4 Diabetic ketoacidosis 182
9.3.5 Chronic renal failure 183
9.3.6 Iatrogenic effects 183
9.3.7 Drug effects 183
9.4 Analysis 184
9.4.1 Specimen 184
9.4.2 Methods and instrumentation 184
9.5 Questions and answers 187
References 188
10 Natriuretic peptides 197
10.1 Case studies 197
10.1.1 Patient A 197
10.1.2 Patient B 198
10.1.3 Patient C 198
10.1.4 Patient D 199
10.1.5 Patient E 200
10.1.6 Patient F 201
10.2 Biochemistry and physiology of cardiac natriuretic peptides 201
10.3 Chemical pathology of natriuretic peptides 202
10.3.1 BNP in diagnosis of symptomatic HF patients 203
10.3.2 Prognosis and risk stratification of HF patients 203
10.3.3 BNP and NT-proBNP as prognostic risk markers in acute coronary syndrome patients 204
10.3.4 Recommendations for use of Biochemical markers in heart failure 204
10.4 Analytical measurements of BNP and NT-proBNP 204
10.4.1 Desired specimens 204
10.4.2 Considerations for measurements of BNP and NT-proBNP 205
10.4.3 Methods for measurements 206
10.5 Questions and answers 207
References 208
Index 211