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. 1973 Dec;37(4):453–478. doi: 10.1128/br.37.4.453-478.1973

Aldolase of lactic acid bacteria: a case history in the use of an enzyme as an evolutionary marker.

J London, K Kline
PMCID: PMC413831  PMID: 4203394

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ANFINSEN C. B., AQVIST S. E., COOKE J. P., JONSSON B. A comparative study of the structures of bovine and ovine pancreatic ribonucleases. J Biol Chem. 1959 May;234(5):1118–1123. [PubMed] [Google Scholar]
  2. Abo-Elnaga I. G., Kandler O. Zur Taxonomie der Gattung Lactobacillus Beijerinck. I. Das Subgenus Streptobacterium Orla Jensen. Zentralbl Bakteriol Parasitenkd Infektionskr Hyg. 1965 Feb 25;119(1):1–36. [PubMed] [Google Scholar]
  3. Air G. M., Thompson E. O., Richardson B. J., Sharman G. B. Amino-acid sequences of kangaroo myoglobin and haemoglobin and the date of marsupial-eutherian divergence. Nature. 1971 Feb 5;229(5284):391–394. doi: 10.1038/229391a0. [DOI] [PubMed] [Google Scholar]
  4. Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Arnheim N., Prager E. M., Wilson A. C. Immunological prediction of sequence differences among proteins. Chemical comparison of chicken, quail, and phesant lysozymes. J Biol Chem. 1969 Apr 25;244(8):2085–2094. [PubMed] [Google Scholar]
  6. Baptist J. N., Shaw C. R., Mandel M. Comparative zone electrophoresis of enzymes of Pseudomonas solanacearum and Pseudomonas cepacia. J Bacteriol. 1971 Nov;108(2):799–803. doi: 10.1128/jb.108.2.799-803.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Baptist J. N., Shaw C. R., Mandel M. Zone electrophoresis of enzymes in bacterial taxonomy. J Bacteriol. 1969 Jul;99(1):180–188. doi: 10.1128/jb.99.1.180-188.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Brenner D. J., Fanning G. R., Johnson K. E., Citarella R. V., Falkow S. Polynucleotide sequence relationships among members of Enterobacteriaceae. J Bacteriol. 1969 May;98(2):637–650. doi: 10.1128/jb.98.2.637-650.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. COHN M., TORRIANI A. M. The relationships in biosynthesis of the beta-galactosidase- and Pz-proteins in Escherichia coli. Biochim Biophys Acta. 1953 Feb;10(2):280–289. doi: 10.1016/0006-3002(53)90251-0. [DOI] [PubMed] [Google Scholar]
  10. Canale-Parola E. Biology of the sugar-fermenting Sarcinae. Bacteriol Rev. 1970 Mar;34(1):82–97. doi: 10.1128/br.34.1.82-97.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Chrambach A., Rodbard D. Polyacrylamide gel electrophoresis. Science. 1971 Apr 30;172(3982):440–451. doi: 10.1126/science.172.3982.440. [DOI] [PubMed] [Google Scholar]
  12. Cocks G. T., Wilson A. C. Enzyme evolution in the Enterobacteriaceae. J Bacteriol. 1972 Jun;110(3):793–802. doi: 10.1128/jb.110.3.793-802.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Cocks G. T., Wilson A. C. Immunological detection of single amino acid substitutions in alkaline phosphatase. Science. 1969 Apr 11;164(3876):188–189. doi: 10.1126/science.164.3876.188. [DOI] [PubMed] [Google Scholar]
  14. Crick F. H. Codon--anticodon pairing: the wobble hypothesis. J Mol Biol. 1966 Aug;19(2):548–555. doi: 10.1016/s0022-2836(66)80022-0. [DOI] [PubMed] [Google Scholar]
  15. Crick F. H. The origin of the genetic code. J Mol Biol. 1968 Dec;38(3):367–379. doi: 10.1016/0022-2836(68)90392-6. [DOI] [PubMed] [Google Scholar]
  16. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  17. Dubnau D., Smith I., Morell P., Marmur J. Gene conservation in Bacillus species. I. Conserved genetic and nucleic acid base sequence homologies. Proc Natl Acad Sci U S A. 1965 Aug;54(2):491–498. doi: 10.1073/pnas.54.2.491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. GORDON R. E., MIHM J. M. A comparative study of some strains received as nocardiae. J Bacteriol. 1957 Jan;73(1):15–27. doi: 10.1128/jb.73.1.15-27.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Gasser F. Electrophoretic characterization of lactic dehydrogenases in the genus Lactobacillus. J Gen Microbiol. 1970 Aug;62(2):223–239. doi: 10.1099/00221287-62-2-223. [DOI] [PubMed] [Google Scholar]
  20. Gasser F., Gasser C. Immunological relationships among lactic dehydrogenases in the genera Lactobacillus and Leuconostoc. J Bacteriol. 1971 Apr;106(1):113–125. doi: 10.1128/jb.106.1.113-125.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Gasser F., Mandel M., Rogosa M. Lactobacillus jensenii sp.nov., a new representative of the subgenus Thermobacterium. J Gen Microbiol. 1970 Aug;62(2):219–222. doi: 10.1099/00221287-62-2-219. [DOI] [PubMed] [Google Scholar]
  22. Gordon J., Schweiger M., Krisko I., Williams C. A. Specificity and evolutionary divergence of the antigenic structure of the polypeptide chain elongation factors. J Bacteriol. 1969 Oct;100(1):1–4. doi: 10.1128/jb.100.1.1-4.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. HOOK W. A., MUSCHEL L. H. ANTICOMPLEMENTARY EFFECTS AND COMPLEMENT ACTIVITY OF HUMAN SERA. Proc Soc Exp Biol Med. 1964 Oct;117:292–297. doi: 10.3181/00379727-117-29561. [DOI] [PubMed] [Google Scholar]
  24. Jensen R. A. Taxonomic implications of temperature dependence of the allosteric inhibition of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase in Bacillus. J Bacteriol. 1970 May;102(2):489–497. doi: 10.1128/jb.102.2.489-497.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Keudell K. C., Goldberg H. S. Dehydrogenase patterns in the study of Bacteroidaceae. Appl Microbiol. 1970 Mar;19(3):505–511. doi: 10.1128/am.19.3.505-511.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. King J. L., Jukes T. H. Non-Darwinian evolution. Science. 1969 May 16;164(3881):788–798. doi: 10.1126/science.164.3881.788. [DOI] [PubMed] [Google Scholar]
  27. Kingsbury D. T., Fanning G. R., Johnson K. E., Brenner D. J. Thermal stability of interspecies Neisseria DNA duplexes. J Gen Microbiol. 1969 Feb;55(2):201–208. doi: 10.1099/00221287-55-2-201. [DOI] [PubMed] [Google Scholar]
  28. Krulwich T. A., Ensign J. C., Tipper D. J., Strominger J. L. Sphere-rod morphogenesis in Arthrobacter crystallopoietes. I. Cell wall composition and polysaccharides of the peptidoglycan. J Bacteriol. 1967 Sep;94(3):734–740. doi: 10.1128/jb.94.3.734-740.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. London J., Meyer E. Y., Kulczyk S. R. Detection of relationships between Streptococcus faecalis and Lactobacillus casei by immunological studies with two forms of malic enzyme. J Bacteriol. 1971 Oct;108(1):196–201. doi: 10.1128/jb.108.1.196-201.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. London J., Meyer E. Y., Kulczyk S. Comparative biochemical and immunological study of malic enzyme from two species of lactic acid bacteria: evolutionary implications. J Bacteriol. 1971 Apr;106(1):126–137. doi: 10.1128/jb.106.1.126-137.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. London J. Regulation and function of lactate oxidation in Streptococcus faecium. J Bacteriol. 1968 Apr;95(4):1380–1387. doi: 10.1128/jb.95.4.1380-1387.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. LéJohn H. B. D(-)-lactate dehydrogenases in fungi. Kinetics and allosteric inhibition by guanosine triphosphate. J Biol Chem. 1971 Apr 10;246(7):2116–2126. [PubMed] [Google Scholar]
  33. MCLEAN R. A., SULZBACHER W. L. Microbacterium thermosphactum, spec: nov.; a nonheat resistant bacterium from fresh pork sausage. J Bacteriol. 1953 Apr;65(4):428–433. doi: 10.1128/jb.65.4.428-433.1953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Mandel M. New approaches to bacterial taxonomy: perspective and prospects. Annu Rev Microbiol. 1969;23:239–274. doi: 10.1146/annurev.mi.23.100169.001323. [DOI] [PubMed] [Google Scholar]
  35. Margoliash E., Nisonoff A., Reichlin M. Immunological activity of cytochrome c. I. Precipitating antibodies to monomeric vertebrate cytochromes c. J Biol Chem. 1970 Mar 10;245(5):931–939. [PubMed] [Google Scholar]
  36. McFadden B. A., Denend A. R. Ribulose diphosphate carboxylase from autotrophic microorganisms. J Bacteriol. 1972 May;110(2):633–642. doi: 10.1128/jb.110.2.633-642.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Miller A., 3rd, Sandine W. E., Elliker P. R. Deoxyribonucleic acid homology in the genus Lactobacillus. Can J Microbiol. 1971 May;17(5):625–634. doi: 10.1139/m71-102. [DOI] [PubMed] [Google Scholar]
  38. Murphy T. M., Mills S. E. Immunochemical and enzymatic comparisons of the tryptophan synthase alpha subunits from five species of Enterobacteriaceae. J Bacteriol. 1969 Mar;97(3):1310–1320. doi: 10.1128/jb.97.3.1310-1320.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. NIRENBERG M. W., MATTHAEI J. H. The dependence of cell-free protein synthesis in E. coli upon naturally occurring or synthetic polyribonucleotides. Proc Natl Acad Sci U S A. 1961 Oct 15;47:1588–1602. doi: 10.1073/pnas.47.10.1588. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Nolan C., Margoliash E. Comparative aspects of primary structures of proteins. Annu Rev Biochem. 1968;37:727–790. doi: 10.1146/annurev.bi.37.070168.003455. [DOI] [PubMed] [Google Scholar]
  41. Phillips A. W., Boyd J. W., Ferguson D. A., Jr, Marucci A. A. Immunochemical comparison of L-asparaginases from Serratia marcescens and Escherichia coli. J Bacteriol. 1971 Aug;107(2):461–467. doi: 10.1128/jb.107.2.461-467.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Prager E. M., Wilson A. C. The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. II. Comparison of precipitin and micro-complement fixation results. J Biol Chem. 1971 Nov 25;246(22):7010–7017. [PubMed] [Google Scholar]
  43. REICHLIN M., HAY M., LEVINE L. ANTIBODIES TO HUMAN A1 HEMOGLOBIN AND THEIR REACTION WITH A2, S, C, AND H HEMOGLOBINS. Immunochemistry. 1964 Apr;1:21–30. doi: 10.1016/0019-2791(64)90052-7. [DOI] [PubMed] [Google Scholar]
  44. RUTTER W. J. EVOLUTION OF ALDOLASE. Fed Proc. 1964 Nov-Dec;23:1248–1257. [PubMed] [Google Scholar]
  45. Rocha V., Crawford I. P., Mills S. E. Comparative immunological and enzymatic study of the tryptophan synthetase beta 2 subunit in the Enterobacteriaceae. J Bacteriol. 1972 Jul;111(1):163–168. doi: 10.1128/jb.111.1.163-168.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Rohlfing S. R., Crawford I. P. Purification and characterization of the beta-galactosidase of Aeromonas formicans. J Bacteriol. 1966 Mar;91(3):1085–1097. doi: 10.1128/jb.91.3.1085-1097.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Sadoff H. L., Hitchins A. D., Celikkol E. Properties of fructose 1,6-diphosphate aldolases from spores and vegetative cells of Bacillus cereus. J Bacteriol. 1969 Jun;98(3):1208–1218. doi: 10.1128/jb.98.3.1208-1218.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Sarich V. M., Wilson A. C. Quantitative immunochemistry and the evolution of primate albumins: micro-complement fixation. Science. 1966 Dec 23;154(3756):1563–1566. doi: 10.1126/science.154.3756.1563. [DOI] [PubMed] [Google Scholar]
  49. Simonds J., Hansen P. A., Lakshmanan S. Deoxyribonucleic acid hybridization among strains of lactobacilli. J Bacteriol. 1971 Jul;107(1):382–384. doi: 10.1128/jb.107.1.382-384.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Singer C. E., Ames B. N. Sunlight ultraviolet and bacterial DNA base ratios. Science. 1970 Nov 20;170(3960):822–825. doi: 10.1126/science.170.3960.822. [DOI] [PubMed] [Google Scholar]
  51. Stanier R. Y., Wachter D., Gasser C., Wilson A. C. Comparative immunological studies of two Pseudomonas enzymes. J Bacteriol. 1970 May;102(2):351–362. doi: 10.1128/jb.102.2.351-362.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Steffen D. L., Cocks G. T., Wilson A. C. Micro-complement fixation in Klebsiella classification. J Bacteriol. 1972 Jun;110(3):803–808. doi: 10.1128/jb.110.3.803-808.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Stevenson R. M., LéJohn H. B. Glutamic dehydrogenases of Oomycetes. Kinetic mechanism and possible vvolutionary history. J Biol Chem. 1971 Apr 10;246(7):2127–2135. [PubMed] [Google Scholar]
  54. WASSERMAN E., LEVINE L. Quantitative micro-complement fixation and its use in the study of antigenic structure by specific antigen-antibody inhibition. J Immunol. 1961 Sep;87:290–295. [PubMed] [Google Scholar]
  55. WATSON J. D., CRICK F. H. Genetical implications of the structure of deoxyribonucleic acid. Nature. 1953 May 30;171(4361):964–967. doi: 10.1038/171964b0. [DOI] [PubMed] [Google Scholar]
  56. WILSON A. C., KAPLAN N. O., LEVINE L., PESCE A., REICHLIN M., ALLISON W. S. EVOLUTION OF LACTIC DEHYDROGENASES. Fed Proc. 1964 Nov-Dec;23:1258–1266. [PubMed] [Google Scholar]
  57. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  58. Whiteside T. L., De Siervo A. J., Salton M. R. Use of antibody to membrane adenosine triphosphatase in the study of bacterial relatioships. J Bacteriol. 1971 Mar;105(3):957–967. doi: 10.1128/jb.105.3.957-967.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Williams R. A., Sadler S. A. Electrophoresis of glucose-6-phosphate dehydrogenase, cell wall composition and the taxonomy of heterofermentative lactobacilli. J Gen Microbiol. 1971 Mar;65(3):351–358. doi: 10.1099/00221287-65-3-351. [DOI] [PubMed] [Google Scholar]

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