E-Book, Englisch, 212 Seiten
Kazmierczak / Azzazy Diagnostic Enzymology
2. fully revised and extended Auflage 2014
ISBN: 978-3-11-022780-2
Verlag: De Gruyter
Format: PDF
Kopierschutz: 1 - PDF Watermark
E-Book, Englisch, 212 Seiten
ISBN: 978-3-11-022780-2
Verlag: De Gruyter
Format: PDF
Kopierschutz: 1 - PDF Watermark
This book is the 2 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.
Zielgruppe
Laboratorians, Medical Technologists, Clinical Biochemists, Clini
Autoren/Hrsg.
Fachgebiete
Weitere Infos & Material
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
14.1.3;6.1.3 Patient C;123
14.1.4;6.1.4 Patient D;124
14.1.5;6.1.5 Patient E;125
14.2;6.2 Biochemistry and physiology;126
14.2.1;6.2.1 Molecular forms;126
14.2.2;6.2.2 CK isoenzymes, atypical forms, and isoforms;127
14.2.3;6.2.3 Reference range;130
14.3;6.3 Chemical pathology;130
14.3.1;6.3.1 Heart disease;130
14.3.2;6.3.2 Skeletal muscle disease;132
14.3.3;6.3.3 Trauma;132
14.4;6.4 Analytical measurement of total CK and CK-MB;133
14.5;6.5 Questions and answers;134
15;References;135
16;7 Gamma-glutamyl transferase;137
16.1;7.1 Case studies;137
16.1.1;7.1.1 Patient A;137
16.1.2;7.1.2 Patient B;137
16.1.3;7.1.3 Patient C;138
16.1.4;7.1.4 Patient D;139
16.1.5;7.1.5 Patient E;140
16.2;7.2 Biochemistry and physiology;140
16.2.1;7.2.1 Molecular forms and post-translational modification;140
16.2.2;7.2.2 Biochemical function;141
16.2.3;7.2.3 Tissue activities and concentrations;141
16.2.4;7.2.4 Metabolic clearance;142
16.2.5;7.2.5 Reference intervals;142
16.3;7.3 Chemical pathology;142
16.3.1;7.3.1 Causes of increased or decreased concentrations or activities;142
16.3.2;7.3.2 Diagnostic utility of GGT;143
16.4;7.4 Analysis;147
16.4.1;7.4.1 Specimen and stability;147
16.4.2;7.4.2 Preferred method for GGT activity;147
16.5;7.5 Questions and answers;148
17;References;148
18;8 Lactate dehydrogenase;151
18.1;9.1 Case studies;151
18.1.1;8.1.1 Patient A;151
18.1.2;8.1.2 Patient B;152
18.1.3;8.1.3 Patient C;153
18.1.4;8.1.4 Patient D;154
18.1.5;8.1.5 Patient E;155
18.2;8.2 Biochemistry and physiology;156
18.2.1;8.2.1 Physiological function;156
18.2.2;8.2.2 Tissue sources;156
18.2.3;8.2.3 Reference ranges;157
18.3;8.3 Chemical pathology;157
18.3.1;8.3.1 Cardiology;158
18.3.2;8.3.2 Hepatology;158
18.3.3;8.3.3 Hematology;158
18.3.4;8.3.4 Oncology;159
18.3.5;8.3.5 Neurology;159
18.3.6;8.3.6 Macro-LD;160
18.3.7;8.3.7 Genetic deficiencies;160
18.4;8.4 Analysis;160
18.4.1;8.4.1 LD isoenzyme determination;161
18.4.2;8.4.2 IFCC reference method;161
18.4.3;8.4.3 Specimen;162
18.5;8.5 Questions and answers;162
19;References;163
20;9 Pancreatic lipase;169
20.1;9.1 Case studies;169
20.1.1;9.1.1 Patient A;169
20.1.2;9.1.2 Patient B;170
20.1.3;9.1.3 Patient C;171
20.1.4;9.1.4 Patient D;172
20.2;9.2 Biochemistry and physiology;173
20.2.1;9.2.1 Molecular forms;173
20.2.2;9.2.2 Molecular structure and tissue expression;174
20.2.3;9.2.3 Mechanism of catalysis;175
20.2.4;9.2.4 Functional regulation;175
20.2.5;9.2.5 Lipase in serum;177
20.2.6;9.2.6 Other lipases;178
20.2.7;9.2.7 Reference range and standardization;180
20.3;9.3 Chemical pathology;180
20.3.1;9.3.1 Acute pancreatitis;180
20.3.2;9.3.2 Pancreatic cancer;181
20.3.3;9.3.3 Cystic fibrosis;182
20.3.4;9.3.4 Diabetic ketoacidosis;182
20.3.5;9.3.5 Chronic renal failure;183
20.3.6;9.3.6 Iatrogenic effects;183
20.3.7;9.3.7 Drug effects;183
20.4;9.4 Analysis;184
20.4.1;9.4.1 Specimen;184
20.4.2;9.4.2 Methods and instrumentation;184
20.5;9.5 Questions and answers;187
21;References;188
22;10 Natriuretic peptides;197
22.1;10.1 Case studies;197
22.1.1;10.1.1 Patient A;197
22.1.2;10.1.2 Patient B;198
22.1.3;10.1.3 Patient C;198
22.1.4;10.1.4 Patient D;199
22.1.5;10.1.5 Patient E;200
22.1.6;10.1.6 Patient F;201
22.2;10.2 Biochemistry and physiology of cardiac natriuretic peptides;201
22.3;10.3 Chemical pathology of natriuretic peptides;202
22.3.1;10.3.1 BNP in diagnosis of symptomatic HF patients;203
22.3.2;10.3.2 Prognosis and risk stratification of HF patients;203
22.3.3;10.3.3 BNP and NT-proBNP as prognostic risk markers in acute coronary syndrome patients;204
22.3.4;10.3.4 Recommendations for use of Biochemical markers in heart failure;204
22.4;10.4 Analytical measurements of BNP and NT-proBNP;204
22.4.1;10.4.1 Desired specimens;204
22.4.2;10.4.2 Considerations for measurements of BNP and NT-proBNP;205
22.4.3;10.4.3 Methods for measurements;206
22.5;10.5 Questions and answers;207
23;References;208
24;Index;211
