Chapter 45 Vitamin B12

Principles of Medical Biology

Volumn 8, Issue C, 1997, Pages 897-917

  Glusker, Jenny P ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

EID: 76249111081     PISSN: 15692582     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2582(97)80106-7     Document Type: Article

References (105)

1. Abeles R.H., Brownstein A.M., and Randles C.H. β-Hydroxypropionaldehyde, an intermediate in the formation of 1,3-propanediol by Aerobacter aerogenes. Biochim. Biophys. Acta 41 (1960) 530-531
2. Addison T. Anaemia: Disease of the supra-renal capsules. Lond. Med. Gaz. 43 (1849) 517-518
3. Addison T. On the Constitutional and Local Effects of Disease of the Supra-renal Capsules (1855), Samuel Highley, London
4. 12-binding proteins using affinity chromatography. I. Purification and properties of human intrinsic factor. J. Biol. Chem. 248 (1973) 3660-3669
5. 12 by the cobalamin-specific intrinsic factor. Febs. Lett. 281 (1991) 90-92
6. 12. J. Biol. Chem. 261 (1986) 3958-3964
7. Babior B.M. The mechanism of adenosylcobalamin-dependent rearrangements. Biofactors 1 (1988) 21-26
8. 12 concentrations in the elderly: A regional study. New Zealand Medical J. 102 (1989) 402-404
9. 12. Proc. Natl. Acad. Sci. USA 44 (1958) 1093-1097
10. 12. Science 264 (1994) 1551-1557
11. Beck W.S. Cobalamin as coenzyme: a twisting trail of research. Amer. J. Hematology 34 (1990) 83-89
12. Biermer A. Einen Vortrag über eine von ihm öfters beobachtete eigenthümliche Form von progressiver perniciöser Anämie, welche mit Verfettungsvorgängen in den Circulationswegen und dadurch mit capillären Blutungen der Haut, Retina, des Gehirns, der Hirnhäute und anderer seröser Membranen einherzugehen pflegt. Kblatt. Schweiz. Arzte 2 (1872) 15-18
13. 12 group. Part IV. The isolation of crystalline nucleotide-free degradation products. J. Chem. Soc. (1957) 1148-1158
14. 12 group. Part V. The structure of the chromophoric grouping. J. Chem. Soc. (1957) 1158-1168
15. 12 coenzyme at 15 K: structure analysis and comparison with the structure at 279 K. Acta Cryst. B49 (1993) 79-89
16. 12 Vol. 2 (1982), Wiley-Interscience, New York 31-55
17. Bresciani-Pahor N., Marzilli L.G., Randaccio L., Toscano P.J., and Zangrando E. Structural determination of a cobalt(III) complex with a Co to tertiary carbon bond: How long can a Co-C bond be?. J. Chem. Soc., Chem. Commun. (1984) 1508-1510
18. 12. Nature (London) 174 (1954) 1169-1170
19. Cahn A., and von Mehring J. Die Säuren des gesunden und kranken Magens. Deutsches. Archiv. fur Klinische Medizin 39 (1886) 233-253
20. Castle W.B. Observations on the etiologic relationship of achylia gastrica to pernicious anemia. I. The effect of the administration to patients with pernicious anemia of the contents of the normal human stomach recovered after the ingestion of beef muscle. Am. J. Med. Sci. 178 (1929) 748-764
21. Castle W.B. Medical progress; development of knowledge concerning gastric intrinsic factor and its relation to pernicious anemia. New Engl. J. Med. 249 (1953) 603-614
22. Castle W.B., and Townsend W.C. Observations on the etiologic relationship of achylia gastrica to pernicious anemia. II. The effect of the administration to patients with pernicious anemia of beef muscle after incubation with normal human gastric juice. Am. J. Med. Sci. 178 (1929) 764-777
23. Castle W.B., Townsend W.C., and Heath C.W. Observations on the etiologic relationship of achylia gastrica to pernicious anemia. III. The nature of the reaction between normal human gastric juice and beef muscle leading to clinical improvement and increased blood formation similar to the effect of liver feeding. Am. J. Med. Sci. 180 (1930) 305-335
24. Christensen J.M., Hippe E., Olesen H., Rye M., Haber E., Lee L., and Thomsen J. Purification of human intrinsic factor by affinity chromatography. Biochim. Biophys. Acta 303 (1973) 319-332
25. Combe J.S. History of a case of anaemia. Trans. Med.-Chirurg Soc. Edinburgh 1 (1824) 194-204
26. 12-dependent enzymic reactions. Phil. Trans. Roy. Soc. (London)-Series B: Biological Sciences 311 (1985) 531-544
27. 12 (1982), John Wiley & Sons, Inc., New York
28. 12-dependent enzymes. Curr. Opin. Struct. Biol. 4 (1994) 919-929
29. 12-binding domains of methionine synthase. Science 266 (1994) 1669-1674
30. Ehrlich P. Farbenanalytische Untersuchungen zur Histologie und Klinik des Blutes (1891), Hirschwald, Berlin
31. 12 by acid hydrolysis. J. Pharm. Pharmacol. (London) 1 (1949) 287-291
32. 12 problems in corrin synthesis. Chem. Soc. Rev. 5 (1976) 377-410
33. 12: Experiments concerning the origin of its molecular structure. Angew. Chem. Int. Ed. Engl. 27 (1988) 5-39
34. 12. Science 196 (1977) 1410-1420
35. Fantes K.H., Page J.E., Parker L.F.J., and Smith E.L. Crystalline anti-pernicious factor from liver. Proc. Roy. Soc. (London) B136 (1949) 592-613
36. July 21. Fenwick S. On atrophy of the stomach in relation to pernicious anemia. Lancet 2 (1870) 78-80
37. Finke R.G., and Hay B.P. Thermolysis of adenosylcobalamin: A product, kinetic and Co-C5′ bond dissociation study. Inorg. Chem. 23 (1984) 3041-3043
38. 12. J. Inorg. Biochem. 40 (1990) 19-22
39. Flint A. A clinical lecture on anaemia. Am. Med. Times 1 (1860) 181-186
40. 12 Vol. 1 (1982), Wiley-Interscience, New York 1-15
41. 12 catalyzed dehydration of 1,2-dihydroxyethane. J. Am. Chem. Soc. 117 (1995) 10131-10132
42. 12 Vol. 1 (1982), Wiley-Interscience, New York 23-106
43. 12 coenzymes. Vitamins and Hormones 50 (1995) 1-76
44. 12 mystery. Chemistry in Britain (1990) 950-954
45. 12 complexes, from human gastric juice. Biochim. Biophys. Acta 127 (1966) 47-58
46. Guest J.R., Friedman S., Woods D.D., and Smith E.L. A methyl analogue of cobamide coenzyme in relation to methionine synthesis by bacteria. Nature (London) 195 (1962) 340-342
47. 12-dependent rearrangements. Science 227 (1985) 869-875
48. 12. J. Am. Chem. Soc. 106 (1984) 8317-8319
49. 12-ethanolamine ammonial lyase: Evidence for a radical mechanism. Science 263 (1994) 958-960
50. Hay B.P., and Finke R.G. Thermolysis of the Co-C bond in adenosylcorrins. 3. Quantification of the axial base effect in adenosylcobalamin by the synthesis and thermolysis of axial base-free adenosylcobinamide. Insights into the energetics of enzyme-assisted cobalt-carbon homolysis. J. Am. Chem. Soc. 109 (1987) 8012-8018
51. Hodgkin D.C., Porter M.W., and Spiller R.C. Crystallographic measurements of the antipernicious anemia factor. Proc. Roy. Soc. (London) B136 (1950) 609-613
52. 12 and the molecular structure of the vitamin. Nature (London) 276 (1995) 325-328
53. 12. Nature (London) 173 (1956) 64-66
54. 12. Proc. Roy. Soc. A424 (1957) 228-263
55. 12. Proc. Roy. Soc. A251 (1959) 306-352
56. 12. Proc. Roy. Soc. A266 (1962) 475-493
57. 12. Proc. Roy. Soc. A266 (1962) 494-517
58. 12 derivative cob(II)alamin. J. Amer. Chem. Soc. 113 (1991) 4523-4530
59. 12-dependent methionine synthetase on the subcellular distribution of folate coenzymes in rat liver. Arch. Biochem. Biophys. 270 (1989) 729-733
60. Jaffe E.K. Predicting the Zn(II) ligands in metalloproteins: Case study, porphobilinogen synthase. Comments Inorg. Chem. 15 (1993) 67-93
61. 12. Nature (London) 276 (1955) 551-553
62. Karlson P. W. B. Castle and the 'intrinsic factor.' [50 Years Ago]. Trends Biochem. Sci. 4 (1979) 286
63. 12 chemistry: The crystal and molecular structure of cob(II)alamin. J. Am. Chem. Soc. 111 (1989) 8936-8938
64. 12: Synthesis and solution spectroscopic and crystal structure analysis of cob-cyanoimidazolylcobamide. Inorg. Chem. 33 (1994) 4128-4139
65. Layzer R.B. Myeloneuropathy after prolonged exposure to nitrous oxide. Lancet 2 (1978) 1227-1230
66. Leichtenstern E. Progressive perniciöse Anämie bei Tabeskranken. Deutsche Medicinische Wochenschrift 10 (1884) 849-850
67. 12 coenzyme. Proc. Roy. Soc. (London) A303 (1968) 45-84
68. Lenhert P.G., and Hodgkin D.C. Structure of the 5,6-dimethylbenzimidazoylcobamide coenzyme. Nature (London) 192 (1961) 937-938
69. Li N., Seetharam S., Lindemans J., Alpers D.H., Arwert F., and Seetharam B. Isolation and sequence analysis of variant forms of human transcobalamin II. Biochim. Biophys. Acta 1172 (1993) 21-30
70. Lien E.L., Ellenbogen L., Law P.Y., and Wood J.M. Studies on the mechanism of cobalamin binding to hog intrinsic factor. J. Biol. Chem. 249 (1974) 890-894
71. Luschinsky C.L., Drummond J.T., Matthews R.G., and Ludwig M.L. Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli. J. Mol. Biol. 225 (1992) 557-560
72. 12 radicals are generated: The crystal structure of methylmalonyl-coenzyme A mutase at 2resolution. Structure 4 (1996) 339-350
73. Minot G.R., and Murphy W.P. Treatment of pernicious anemia by special diet. J. Am. Med. Assoc. 87 (1926) 470-476
74. 12 Vol. 2 (1982), Wiley-Interscience, New York 57-85
75. Ong S.P., Nelson L.S., and Hogenkamp H.P. Synthesis of 3′-C-methyladenosine and 3′-C-methyluridine diphosphates and their interaction with the ribonucleoside diphosphate reductase from Corynebacterium nephridii. Biochemistry 31 (1992) 11210-11215
76. 12 is coordinated by histidine and not by dimethylbenzimidazole on methylmalonyl-CoA mutase. J. Am. Chem. Soc. 117 (1995) 7033-7034
77. Pepper W. Progressive pernicious anaemia or anhaematosis. Am. J. Med. Sci. 70 Oct. (1875) 313-347
78. Pett V.B., Liebman M.N., Murray-Rust P., Prasad K., and Glusker J.P. Conformational variability of corrins: Some methods of analysis. J. Am. Chem. Soc. 109 (1987) 3207-3215
79. 9 years of coordination chemistry. Pure & Appl. Chem. 65 (1993) 1513-1520
80. Quadros E.V., Rothenberg S.P., Pan Y.C., and Stein S. Purification and molecular characterization of human transcobalamin II. J. Biol. Chem. 261 (1986) 15455-15460
81. Rétey J., and Lynen F. The absolute configuration of methylmalonyl-CoA mutase. Biochem. Biophys. Res. Commun. 16 (1964) 358-361
82. Rétey J., Suckling C.J., Arigoni D., and Babior B.M. The stereochemistry of the reaction catalyzed by ethanolamine ammonia-lyase, an adenosylcobalamin-dependent enzyme. An example of recemization accompanying substitution. J. Biol. Chem. 249 (1974) 6359-6360
83. 12. Science 107 (1948) 396-397
84. Robscheit-Robbins F.S., and Whipple G.H. Blood regeneration in severe anemia: Favorable influence of liver, heart, and skeletal muscle in diet. Am. J. Physiol. 72 (1925) 408-418
85. 12 coenzyme: Methylcobalamin studies by X-ray and NMR methods. J. Am. Chem. Soc. 107 (1985) 1729-1738
86. 2O. Acta Cryst. B43 (1987) 280-295
87. 12. J. Lab. Clin. Med. 42 (1953) 860-866
88. 12-a survey of the last four billion years. Angew. Chemie, Intl. Edn. Engl. 32 (1993) 1223-1243
89. Scetharam B., and Alpers D.H. Isolation of native and proteolytically derived ileal receptor for intrinsic factor-cobalamin. Meth. Enzym. 123 (1986) 23-28
90. Seetharam B., Levine J.S., Ramasamy M., and Alpers D.H. Purification, properties, and immunochemical localization of a receptor for intrinsic factor-cobalamin complex in the rat kidney. J. Biol. Chem. 263 (1988) 4443-4449
91. 12. Science 124 (1956) 272
92. 12 for the growth of Lactobacillus lactis. Science 107 (1948) 397-398
93. Smith E.L. Purification of anti-pernicious anemia factors from liver. Nature (London) 161 (1948) 638-639
94. Smith E.L., and Parker L.F.J. Purification of anti-pernicious anaemia factor. Biochem. J. 43 (1948) viii-ix
95. Stubbe J. Binding site revealed of nature's most beautiful cofactor. Science 266 (1994) 1663-1664
96. 12 in diol dehydrase. Arch. Biochem. Biophys. 242 (1985) 470-477
97. Toraya T., and Ishida A. Acceleration of cleavage of the carbon-cobalt bond of sterically hindered alkylcobalamins by binding to a portion of diol dehydrase. Biochemistry 27 (1988) 7677-7681
98. 12. IX. Crystal structure of cobyric acid, factor Vla. Proc. Roy. Soc. A323 (1971) 455-497
99. 12 coenzymes containing benzimidazole or dimethylbenzimidazole. Proc. Natl. Acad. Sci. USA 45 (1959) 521-525
100. Werthemann L. Untersuchungen and Kobalt(II)-and Kobalt(III/Komplexen des Cobyrin saure-heptamethylester. Diss. No. 4097 (1968), ETH, Switzerland
101. 12 crystals. Proc. Roy. Soc. (London) A266 (1962) 440-474
102. 12 intermediate. Implications for enzyme catalysis. Biophysical J. 63 (1992) 412-417
103. Wolfle K., Michenfelder M., Kâövnig A., Hull W.E., and Rétey J. On the mechanism of action of methylmalonyl-CoA mutase. Change of the steric course on isotope substitution. Eur. J. Biochem. 156 (1986) 545-554
104. 12. Pure and Appl. Chem. 33 (1973) 145-177
105. Woodward R.B., and Hoffmann R. Stereochemistry of electrocyclic reactions. J. Am. Chem. Soc. 87 (1965) 395-397