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E-raamat: Diagnostic Enzymology [De Gruyter e-raamatud]

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  • Formaat: 212 pages, 17 Tables, black and white; 6 Illustrations, black and white; 2 Illustrations, color
  • Sari: de Gruyter Textbook
  • Ilmumisaeg: 14-Apr-2014
  • Kirjastus: De Gruyter
  • ISBN-13: 9783110227802
Teised raamatud teemal:
  • De Gruyter e-raamatud
  • Hind: 1 260,00 €*
  • * hind, mis tagab piiramatu üheaegsete kasutajate arvuga ligipääsu piiramatuks ajaks
Diagnostic EnzymologySuurem pilt
  • Formaat: 212 pages, 17 Tables, black and white; 6 Illustrations, black and white; 2 Illustrations, color
  • Sari: de Gruyter Textbook
  • Ilmumisaeg: 14-Apr-2014
  • Kirjastus: De Gruyter
  • ISBN-13: 9783110227802
Teised raamatud teemal:
Wiley OnlineRohkem infot De Gruyter e-raamatute kohta
Raamatu kodulehekülg: http://dx.doi.org/10.1515/9783110227802

This book is the2nd 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.

Preface v
List of contributing authors vii
1 Angiotensin converting enzyme 1(18)
Joe M. El-Khoury
Edmunds Reineks
Sihe Wang
1.1 Case studies
1(2)
1.1.1 Patient A
1(1)
1.1.2 Patient B
1(1)
1.1.3 Patient C
2(1)
1.2 Biochemistry and physiology
3(4)
1.2.1 Physiological function
3(1)
1.2.2 Biochemistry and molecular forms
3(2)
1.2.3 Tissue sources
5(1)
1.2.4 Reference ranges
5(2)
1.3 Chemical pathology
7(2)
1.3.1 ACE in sarcoidosis
7(2)
1.4 Analysis
9(3)
1.4.1 Specimen
9(1)
1.4.2 Spectrophotometric methods
10(1)
1.4.3 High-performance liquid chromatography
10(1)
1.4.4 Fluorometric methods
11(1)
1.4.5 Radioassays
11(1)
1.4.6 Other methods
11(1)
1.4.7 Inhibitors of ACE
12(1)
1.5 Questions and answers
12(1)
References
13(6)
2 Acetylcholinesterase and butyrylcholinesterase 19(22)
Peter L. Platteborze
2.1 Case studies
19(4)
2.1.1 Patient A
19(1)
2.1.2 Patient B
20(1)
2.1.3 Patient C
21(1)
2.1.4 Patient D
22(1)
2.1.5 Patient E
22(1)
2.2 Biochemistry and physiology of the cholinesterases
23(6)
2.2.1 Molecular forms
23(3)
2.2.2 Inheritance of BChE variants
26(3)
2.3 Chemical pathology
29(7)
2.3.1 Pesticide and nerve agent poisoning
29(7)
2.4 Analytical measurements of AChE and BChE
36(2)
2.4.1 Desired specimens
36(2)
2.5 Questions and answers
38(2)
References
40(1)
3 Aldolase 41(16)
Edmunds Reineks
Joe M. El-Khoury
Sihe Wang
3.1 Case studies
41(2)
3.1.1 Patient A
41(1)
3.1.2 Patient B
42(1)
3.1.3 Patient C
43(1)
3.2 Biochemistry and physiology
43(4)
3.2.1 Physiological function
43(1)
3.2.2 Biochemistry and molecular structure
44(1)
3.2.3 Tissue source(s) and expression of ALD
45(1)
3.2.4 Clearance and metabolism of ALD
45(1)
3.2.5 Reference ranges
46(1)
3.3 Chemical pathology
47(3)
3.3.1 Polymyositis/dermatomyositis
47(1)
3.3.2 Duchenne muscular dystrophy
48(1)
3.3.3 Drug-induced myopathy
48(1)
3.3.4 Pathologies in which CK does not reflect the extent of muscle damage
49(1)
3.4 Analysis
50(2)
3.4.1 Specimen
50(1)
3.4.2 Analyte stability
51(1)
3.4.3 Interferences
51(1)
3.4.4 Reference methods
51(1)
3.5 Questions and answers
52(1)
References
53(4)
4 Alkaline phosphatase 57(24)
Amy E. Schmidt
4.1 Case studies
57(6)
4.1.1 Patient A
57(1)
4.1.2 Patient B
58(1)
4.1.3 Patient C
59(1)
4.1.4 Patient D
60(1)
4.1.5 Patient E
60(1)
4.1.6 Patient F
61(2)
4.2 Biochemistry and physiology
63(5)
4.2.1 Structure
63(3)
4.2.2 Physiological function of ALP in tissue/blood/other fluids
66(1)
4.2.3 Tissue sources of ALP
66(1)
4.2.4 Clearance/metabolism of enzyme
67(1)
4.2.5 Reference ranges
67(1)
4.3 Chemical pathology
68(3)
4.3.1 Liver disease
68(1)
4.3.2 Bone disease
69(1)
4.3.3 Metastatic cancer
69(1)
4.3.4 Miscellaneous pancreatic disorders
69(1)
4.3.5 Cystic fibrosis
70(1)
4.3.6 Chronic renal failure
70(1)
4.3.7 Drug therapy
70(1)
4.3.8 Miscellaneous
71(1)
4.4 Analysis
71(4)
4.4.1 Technical problems
71(1)
4.4.2 Reference method
72(1)
4.4.3 Isoenzyme analysis
72(3)
4.5 Questions and answers
75(1)
Acknowledgements
75(1)
References
76(5)
5 Aspartate aminotransferase and alanine aminotransferase 81(24)
Joe M. El-Khoury
Sihe Wang
5.1 Case studies
81(3)
5.1.1 Patient A
81(1)
5.1.2 Patient B
82(1)
5.1.3 Patient C
82(1)
5.1.4 Patient D
83(1)
5.1.5 Patient E
84(1)
5.2 Biochemistry and physiology
84(5)
5.2.1 Molecular forms
84(2)
5.2.2 Biochemical function
86(1)
5.2.3 Normal physiology
86(2)
5.2.4 Reference ranges
88(1)
5.3 Chemical pathology
89(6)
5.3.1 Liver disease
89(3)
5.3.2 Hemochromatosis
92(1)
5.3.3 Skeletal muscle disease
93(1)
5.3.4 Heart disease
94(1)
5.3.5 Other causes of AST increase
95(1)
5.4 Analysis
95(2)
5.4.1 Specimens
95(1)
5.4.2 Reaction used
95(1)
5.4.3 Interferences
96(1)
5.4.4 Methods for AST isoenzymes
97(1)
5.5 Questions and answers
97(1)
References
98(7)
6 Creatine kinase, isoenzymes, and isoforms 105(16)
Alan H.B. Wu
6.1 Case studies
105(5)
6.1.1 Patient A
105(1)
6.1.2 Patient B
106(1)
6.1.3 Patient C
107(1)
6.1.4 Patient D
108(1)
6.1.5 Patient E
109(1)
6.2 Biochemistry and physiology
110(4)
6.2.1 Molecular forms
110(1)
6.2.2 CK isoenzymes, atypical forms, and isoforms
111(3)
6.2.3 Reference range
114(1)
6.3 Chemical pathology
114(3)
6.3.1 Heart disease
114(2)
6.3.2 Skeletal muscle disease
116(1)
6.3.3 Trauma
116(1)
6.4 Analytical measurement of total CK and CK-MB
117(1)
6.5 Questions and answers
118(1)
References
119(2)
7 Gam ma-glutamyl transferase 121(14)
Sarah M. Brown
7.1 Case studies
121(3)
7.1.1 Patient A
121(1)
7.1.2 Patient B
121(1)
7.1.3 Patient C
122(1)
7.1.4 Patient D
123(1)
7.1.5 Patient E
124(1)
7.2 Biochemistry and physiology
124(2)
7.2.1 Molecular forms and post-translational modification
124(1)
7.2.2 Biochemical function
125(1)
7.2.3 Tissue activities and concentrations
125(1)
7.2.4 Metabolic clearance
126(1)
7.2.5 Reference intervals
126(1)
7.3 Chemical pathology
126(5)
7.3.1 Causes of increased or decreased concentrations or activities
126(1)
7.3.2 Diagnostic utility of GGT
127(4)
7.4 Analysis
131(1)
7.4.1 Specimen and stability
131(1)
7.4.2 Preferred method for GGT activity
131(1)
7.5 Questions and answers
132(1)
References
132(3)
8 Lactate dehydrogenase 135(18)
Olajumoke Oladipo
Dennis J. Dietzen
8.1 Case studies
135(5)
8.1.1 Patient A
135(1)
8.1.2 Patient B
136(1)
8.1.3 Patient C
137(1)
8.1.4 Patient D
138(1)
8.1.5 Patient E
139(1)
8.2 Biochemistry and physiology
140(1)
8.2.1 Physiological function
140(1)
8.2.2 Tissue sources
140(1)
8.2.3 Reference ranges
141(1)
8.3 Chemical pathology
141(3)
8.3.1 Cardiology
142(1)
8.3.2 Hepatology
142(1)
8.3.3 Hematology
142(1)
8.3.4 Oncology
143(1)
8.3.5 Neurology
143(1)
8.3.6 Macro-LD
144(1)
8.3.7 Genetic deficiencies
144(1)
8.4 Analysis
144(2)
8.4.1 LD isoenzyme determination
145(1)
8.4.2 IFCC reference method
145(1)
8.4.3 Specimen
146(1)
8.5 Questions and answers
146(1)
References
147(6)
9 Pancreatic lipase 153(28)
Wan-Ming Zhang
Edmunds Reineks
Joe M. El-Khoury
Sihe Wang
9.1 Case studies
153(4)
9.1.1 Patient A
153(1)
9.1.2 Patient B
154(1)
9.1.3 Patient C
155(1)
9.1.4 Patient D
156(1)
9.2 Biochemistry and physiology
157(7)
9.2.1 Molecular forms
157(1)
9.2.2 Molecular structure and tissue expression
158(1)
9.2.3 Mechanism of catalysis
159(1)
9.2.4 Functional regulation
159(2)
9.2.5 Lipase in serum
161(1)
9.2.6 Other lipases
162(2)
9.2.7 Reference range and standardization
164(1)
9.3 Chemical-pathology
164(4)
9.3.1 Acute pancreatitis
164(1)
9.3.2 Pancreatic cancer
165(1)
9.3.3 Cystic fibrosis
166(1)
9.3.4 Diabetic ketoacidosis
166(1)
9.3.5 Chronic renal failure
167(1)
9.3.6 Iatrogenic effects
167(1)
9.3.7 Drug effects
167(1)
9.4 Analysis
168(3)
9.4.1 Specimen
168(1)
9.4.2 Methods and instrumentation
168(3)
9.5 Questions and answers
171(1)
References
172(9)
10 Natriuretic peptides 181(14)
Robert H. Christenson
Hassan M.E. Azzazy
10.1 Case studies
181(4)
10.1.1 Patient A
181(1)
10.1.2 Patient B
182(1)
10.1.3 Patient C
182(1)
10.1.4 Patient D
183(1)
10.1.5 Patient E
184(1)
10.1.6 Patient F
185(1)
10.2 Biochemistry and physiology of cardiac natriuretic peptides
185(1)
10.3 Chemical pathology of natriuretic peptides
186(2)
10.3.1 BNP in diagnosis of symptomatic HF patients
187(1)
10.3.2 Prognosis and risk stratification of HF patients
187(1)
10.3.3 BNP and NT-proBNP as prognostic risk markers in acute coronary syndrome patients
188(1)
10.3.4 Recommendations for use of Biochemical markers in heart failure
188(1)
10.4 Analytical measurements of BNP and NT-proBNP
188(3)
10.4.1 Desired specimens
188(1)
10.4.2 Considerations for measurements of BNP and NT-proBNP
189(1)
10.4.3 Methods for measurements
190(1)
10.5 Questions and answers
191(1)
References
192(3)
Index 195
Steven C. Kazmierczak, Health & Science University, Portland, Oregon, USA; Hassan M. E. Azzazy, American University in Cairo, Egypt.
Püsilink: https://www.kriso.ee/db/9783110227802_pe.html