172 Part II: Water, Enzymology, Biotechnology, and Protein Cross-linking
Briggs GE, Haldane JBS. 1925. A note on the kinetics
of enzyme action. Biochem J 19:338–339.
Brocklehurst K, Dixon HBF. 1977. The pH-
dependence of second-order rate constants of en-
zyme modification may provide free-reactant pKa
values. Biochem J 167:859–862.
Brown AJ. 1902. Enzyme action. J Chem Soc 81:373–
386.
Burbaum JJ, Schimmel P. 1991. Structural relation-
ships and the classification of aminoacyl-tRNA syn-
thetases. J Biol Chem 266:16965–16968.
Cardenas ML, Cornish-Bowden A, Ureta T. 1998.
Evolution and regulatory role of the hexokinases.
Biochim Biophys Acta 1401:242–264.
Cherfils J, Vachette P, Janin J. 1990. Modelling al-
losteric processes in E. coliaspartate transcarbamy-
lase. Biochimie 72(8): 617–624.
Clark JB. 1992. In: Eisenthal R, Danson MJ, editors,
Enzyme Assays, A Practical Approach. New York:
Oxford University Press.
Copeland RA. 2000. Enzymes, 2nd edition. New York:
Wiley-VCH Inc.
Cornish-Bowden A. 1995. Fundamentals of Enzyme
Kinetics, 2nd edition. London: Portland Press.
Cornish-Bowden A. 1996. In: Engel PC, editor, En-
zymology Labfax. San Diego: BIOS Scientific Pub-
lishers, Oxford and Academic Press. Pp. 96–113.
Cusack S. 1997. Aminoacyl-tRNA synthetases. Curr
Opin Struct Biol 7(6): 881–889.
Dixon M, Webb EC. 1979. Enzymes. 3rd edition. New
York: Academic Press.
Drake JW. 1999. The distribution of rates of sponta-
neous mutation over viruses, prokaryotes, and euk-
aryotes. Ann N Y Acad Sci. 870:100–107.
Eadie GS. 1942. The inhibition of cholinesterase by
physostigmine and prostigmine. J Biol Chem 146:
85–93.
Eisenthal R, Cornish-Bowden A. 1974. The direct lin-
ear plot. A new graphical procedure for estimating
enzyme parameters. Biochem J 139:715–720.
Fang TY, Ford C. 1998. Protein engineering of
Aspergillus awamoriglucoamylase to increase its
pH optimum. Protein Eng 11:383–388.
Goodman MF. 1997. Hydrogen bonding revisited:
Geometric selection as a principal determinant of
DNA replication fidelity. Proc Natl Acad Sci USA
94:10493–10495.
Gul S, Sreedharan SK, Brocklehurst K. 1998. Enzyme
Assays. Oxford: John Wiley and Sons Ltd.
Hames BD, Rickwood D. 1990. Gel Electrophoresis of
Proteins: A Practical Approach, 2nd edition. Oxford:
IRL Press.
Hammes GG. 2002. Multiple conformational changes
in enzyme catalysis, Biochemistry 41(26): 8221–
8228.
Hanes CS. 1932. Studies on plant amylases. I. The
effect of starch concentration upon the velocity of
hydrolysis by the amylase of germinated barley.
Biochem J 26:1406–1421.
Harlow E, Lane D. 1988. Antibodies: A Laboratory
Manual. NewYork. Cold Spring Harbor: CSHL Press.
Hill AV. 1910. The possible effects of the aggregation
of molecules of hemoglobin on its dissociation
curves. J Physiol 40, 4–7.
Hofstee BHJ. 1959. Non-inverted versus inverted plots
in enzyme kinetics. Nature 184:1296–1298.
Igarashi K, Ozawa T, Ikawa-Kitatama K, Hayashi Y,
Araki H, Endo K, Hagihara H, Ozaki K, Kawai S, Ito
S. 1999. Thermostabilization by proline substitution
in an alkaline, liquefying -amylase from Bacillus
sp. strain KSM-1378. Biosci Biotechnol Biochem
63:1535-1540.
Jacobsen CF et al. 1957. In: Glick D, editor, Methods
of Biochemical Analysis, vol IV. New York:
Interscience Publishers. Pp. 171–210.
Khalifah RG. 2003. Reflections on Edsall’s carbonic
anhydrase: Paradoxes of an ultra fast enzyme.
Biophys Chem. 100:159–170.
Kornberg RD. 1996. RNA polymerase II transcription
control. Trends Biochem Sci 21:325–327.
Lakowicz JR. 1983. Principles of Fluorescence Spec-
troscopy. New York: Plenum Publishing.
Langfort J, Ploug T, Ihlemann J, Enevoldsen LH,
Stallknecht B, Saldo M, Kjaer M, Holm C, Galbo H.- Hormone-sensitive lipase expression and reg-
ulation in skeletal muscle. Adv Exp Med Biol
441:219–228.
Luan S. 2003. Protein phosphatases in plants. Annu
Rev Plant Biol 54:63–92.
Lineweaver H, Burk D. 1934. The determination of
enzyme dissociation constants. J Am Chem Soc 56:
658–666.
Michaelis L, Menten ML. 1913. Die Kinetik der In-
vertinwirkun. Biochem Z 49:333–369.
Nuttall FQ, Gilboe DP, Gannon MC, Niewoehner CB,
Tan AWH. 1988. Regulation of glycogen synthesis
in the liver. Am J Med 85(Supp. 5A): 77–85.
Oldham KG. 1992. In: Eisenthal R, Danson MJ, edi-
tors. Enzyme Assays, A Practical Approach. New
York: Oxford University Press. Pp. 93–122.
Oliver GW, Stetler-Stevenson WG, Kleiner DE. 1999.
In: Sterchi EE, Stöcker W, editors, Proteolytic En-
zymes: Tools and Targets. Berlin Heidelberg:
Springer-Verlag Berlin. Pp. 63–76.