By Jesse P. Greenstein, John T. Edsall

ISBN-10: 1483231240

ISBN-13: 9781483231242

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Academic Press, New York. Greenstein, J. P. (1954). Advances in Protein Chem. 9, 121. STRUCTURE AND FUNCTION OF CARBOXYPEPTIDASE 59 Greenstein, J. P. (1956). " Japanese Biochem. Soc, p. 1. Harris, I. J. (1955). Chem. Soc. (London), Spec. Publ. No. 2, p. 71. Kägi, J. H. R. (1959). Federation Proc. 18, 484. Keller, P. , and Neurath, H. (1956). / . Biol. Chem. 223, 457. Keller, P. , and Neurath, H. (1958a). J. Biol. Chem. 230, 905. Keller, P. , and Neurath, H. (1958b). J. Biol. Chem. 233, 344. Keller, P.

This all-or-none difference in behavior toward phenylacetate suggests that in native carboxypeptidase the metal either coordi­ nates with the inhibitor, or confers a configuration to the enzyme which is essential for the formation of the protein-inhibitor com­ plex. No decision between these alternatives can be made on the basis of the present data. However, regardless of interpretation, these findings strongly suggest that in carboxypeptidase the metal may not only contribute to the catalytic step but is also essential for the formation of the enzyme-substrate complex.

Trav. lab. Carlsberg 15, N o . 7. Linderstr0m-Lang, K. (1955). Chem. Soc. (London), Spec. Publ. No. 2, 1. INTERNAL HYDROGEN BONDING IN RIBONUCLEASE 41 Scheraga, H . A. (1957). Biochim. et Biophys. Acta 23, 196. Scheraga, H . A. (1958). Abstr. 134th Meeting Am. Chem. Soc, Chicago, Illinois, Sept. 1958, p . 51C. Scheraga, H . A. (1959). Ann. Rev. Phys. Chem. 10,191. Scheraga, H . A. (1960). J. Am. Chem. Soc, in press. Scheraga, H . , and Mandelkern, L. (1953). J. Am. Chem. Soc. 75, 179. Schildkraut, C.

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Amino Acids, Proteins and Cancer Biochemistry by Jesse P. Greenstein, John T. Edsall

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