Chemical reagents for protein modification

Chemical Reagents for Protein Modification

Volumn 2, Issue , 2018, Pages 1-178

  Lundblad, Roger L ^a   Noyes, Claudia M ^b  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

^b UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 85053097395     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9781351070539     Document Type: Book

References (570)

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124. Philips, M., Pho, D. B., and Pradel, L.-A., An essential arginyl residue in yeast hexokinase, Biochim. Biophys. Acta, 566, 296, 1979.
125. Mornet, D., Pantel, P., Audemard, E., and Kassab, R., Involvement of an arginyl residue in the catalytic activity of myosin heads, Eur. J. Biochem., 100, 421, 1979.
126. Cheung, S.-T. and Fonda, M. L., Kinetics of the inactivation of Escherichia coli glutamate apodecarboxylase by phenylglyoxal, Arch. Biochem. Biophys., 198, 541, 1979.
127. Davidson, W. S. and Flynn, T. G., A functional arginine residue in NADPH-dependent aldehyde reductase from pig kidney, J. Biol. Chem.. 254, 3724, 1979.
128. Poulose, A. J. and Kolattukudy, P. E., Presence of one essential arginine that specifically binds the 2'-phosphate of NADPH on each of the ketoacyl reductase and enoyl reductase active sites of fatty acid synthetase, Arch. Biochem. Biophys., 199, 457, 1980.
129. Bond, M. W., Chiu, N. Y., and Cooperman, B. S., Identification of an arginine important for enzymatic activity within the covalent structure of yeast inorganic pyrophosphatase, Biochemistry, 19, 94, 1980.
130. Mautner, H. G., Pakula, A. A., and Merrill, R. E., Evidence for presence of an arginine residue in the coenzyme A binding site of choline acetyltransferase, Proc. Natl. Acad. Sci. U.S.A., 78, 7449, 1981.
131. Hayman, S. and Colman, R. F., Effect of arginine modification on the catalytic activity and allosteric activation by adenosine diphosphate of the diphosphopyridine nucleotide specific isocitrate dehydrogenase of pig heart, Biochemistry, 17, 4161, 1978.
132. Varimo, K. and Londesborough, S., Evidence for essential arginine in yeast adenylate cyclase, FEBS Lett., 106, 153, 1979.
133. Malinowski, D. P. and Fridovich, I., Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase, Biochemistry, 18, 5909, 1979.
134. +)-ATPase. I. Essential arginine residue in its substrate binding center, Biochim. Biophys. Acta, 597, 331, 1980.
135. Fujioka, M. and Takata, Y., Role of arginine residue in saccharopine dehydrogenase (L-Lysine Forming) from baker’s yeast, Biochemistry, 20, 468, 1981.
136. Aurebekk, B. and Little, C, Functional arginine in phospholipase C of Bacillus cereus, Int. J. Biochem., 8, 757, 1977.
137. McTigue, J. J. and Van Etten, R. L., An essential arginine residue in human prostatic acid phosphatase, Biochim. Biophys. Acta, 523, 422, 1978.
138. Ferti, C, Curti, B., Simonetta, M. P., Ronchi, S., Galliano, M., and Minchiotti, L., Reactivity of D-amino acid oxidase with 1,2-cyclohexanedione: evidence for one arginine in the substrate binding site, Eur. J. Biochem., 119, 553, 1981.
139. Belfort, M., Maley, G. F., and Maley, F., A single functional arginyl residue involved in the catalysis by Lactobacillus casei thymidylate synthetase. Arch. Biochem. Biophys., 204, 340, 1980.
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