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

By Jesse P. Greenstein, John T. Edsall

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Extra resources for Amino Acids, Proteins and Cancer Biochemistry

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1957a). Arch. Biochem. Biophys. 72, 437 (1957). , Greenstein, J. , and Birnbaum, S. M. (1957b). Arch. Biochem. Biophys. 72, 448. Wretlind, K. A. and Rose, W. C. (1950). J. Biol. Chem. 187, 697. Internal Hydrogen Bonding in Ribonuclease12 H. A. SCHERAGA, C. Y. CHA, J. , and C. L. SCHILDKRAUT Department of Chemistry, Cornell University, Ithaca, New York δ ο MUCH PROGRESS has been made in recent years in the determination of the amino acid sequences of polypeptide chains that it has become feasible to attempt to determine the complete internal structure (secondary and tertiary) of a protein.

FIG. 3. Chromatographie resolution on DEAE-cellulose of the anionic components of activated canine pancreatic juice collected after the administra­ tion of Zn65. ). ) 48 NEURATH, RUPLEY, AND VALLEE 40 0 20 Time of Dialysis in Hours FIG. 4. Rates of loss of zinc and enzymatic activity on dialysis of carboxypeptidase against buffers of low pH. The circles denote per cent zinc inside the dialysis bag, the squares per cent zinc in buffer outside the dialysis bag, and the crosses per cent peptidase activity inside the dialysis bag.

The substrates involved were mainly a-halogenacylated amino acids and simple peptides, and the enzymes included a group of acylases of renal tissue, and pancreatic carboxypeptidase (Greenstein, 1954, 1956). Since in these systems the stereospecificity of the enzymes was practically absolute, this work has led to a new and powerful practical method for the resolution of amino acids by asymmetric hydrolysis. By use of renal acylases I and II, all but four iV-acylamino acids could be resolved to within one part in 1000 or better, whereas pancreatic carboxypeptidase, which in this sense is likewise an acylase, was effectively employed for the resolution of phenylalanine, tyrosine, tryptophan, and ß-phenylserine.

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