By Professor Dr. Dharam P. Agarwal, Professor Dr. H. Werner Goedde (auth.)
Alcohol abuse, alcohol intolerance, alcohol dependence and different alcohol-related disabilities are one of the most not easy public illnesses dealing with our modern day society. the aim of this finished monograph is to study the on hand wisdom in regards to the pharmacogenetic foundation of alcohol sensitivity and its physiolgical implications and to synthesize the majority of present wisdom relating to metabolic good points and biomedical disturbances concerning alcoholism. The chapters conceal a vast array of disciplines together with an summary of ancient and epidemiological features, biochemistry and molecular genetics of enzymes occupied with alcohol metabolism, biochemical and neuropsychopharmacological results of alcohol. significant emphasis is put on the function of genetic components in alcoholism. The experimental information are summarized and a finished bibliography is included.
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Additional resources for Alcohol Metabolism, Alcohol Intolerance, and Alcoholism: Biochemical and Pharmacogenetic Approaches
Braun et a\. 1987b) Alcohol Metabolism: Biochemistry and Genetic Variations 38 10 20 30 M L R A A A A W PAW A P P L VfSlR R HfPlG R A A P N Q Q P SUJS G TLclD 40 L P V L LTD L 10 50 60 E V FeN Q I FIN NEW H D AfSl Rr<] Tr'PJ T VfNPl S T G KI Q Y T 20 KI FIN NEW HD 30 S~GLJK~V FUiJjP 40 AA [Elv 70 80 90 I~A E G D KED V D K ARE G R P G~L G p UJE L~E 50 E G D KED V D 60 K A V K A A R Q~I G~ 70 110 120 IE R D R T Yf""lA L I E R DR L L~T 100 M Fig. 18. Comparison of the first 100 amino acids at the amino-terminal ends of ALDH I (upper sequence) and ALDH II (lower sequence).
These relationships strongly suggest that duplicatory events leading to human class I isozyme differences are different from those leading to differences in horse E and S types. The isozyme divergence in man is a later event than the species separation of man and horse. In man, the a subunit diverged first, and the f3 and y subunits diverged later. J Fig. 7. Relationship between isozyme differences (class I ADH) and species differences (horse E type versus human class I type). Numbers give total amino acid replacement in all the pairwise comparisons, showing the isozyme differences horizontally in the middie, and the species differences above and below.
Likewise, the immune sera raised against purified human ALDH I and II did not react with human ALDH III, emphasizing the separate identity of ALDH III. However, other studies show a lack of such an immunological cross-reaction between human ALDH I and II isozymes and their antibodies (Agarwal et al. 1984; Tipton and Henehan 1984; Johnson et al. 1987). Also, antibodies raised against human erythrocyte isozyme (ALDH II) cross-reacted only with the erythrocyte ALDH isozyme and liver ALDH II isozyme but not with the liver isozyme I (Agarwal et al.
Alcohol Metabolism, Alcohol Intolerance, and Alcoholism: Biochemical and Pharmacogenetic Approaches by Professor Dr. Dharam P. Agarwal, Professor Dr. H. Werner Goedde (auth.)