98 Martynas Ycas 



67. K. Ohno: On the structure of lysozyme. III. On the carboxyl-terminal peptide. /. 

 Biochem. 42, 615-625 (1955). 



68. K. Ohno: On the structure of lysozyme II. Characterization of aspartyl, asparaginyl, 

 and glutaminyl residues in lysozyme. /. Biochem. 41, 345-350 (1954). 



69. I. I. Geschwind, C. H. Li, and L. Barnafi: Isolation and structure of melanocyte- 

 stimulating hormone from porcine pituitary glands. J. Amer. Chein. Soc. 78, 4494-4495 

 (1956). 



70. J. I. Harris and P. Roos: Amino-acid sequence of a melanophore stimulating peptide. 

 Nature, Lond. 178, 90 (1956). 



71. V. M. Ingram: The application of Edman's peptide degradation method to horse 

 myoglobin and haemoglobin. Biochim. Biophys. Acta 16, 599-600 (1955). 



72. M. Flavin and C. B. Anfinsen: The isolation and characterization of cysteic acid 

 peptides in studies on ovalbumin synthesis. /. Biol. Chem. 211, 375-390 (1954). 



73. M. Otessen and A. Wollenberg: Stepwise degradation of the peptides liberated in the 

 transformation of ovalbumin to plakelbumin. C R. Lab. Carhberg (Chim.) 28, 463^75 

 (1953). 



74. M. Flavin: Cysteine and phosphoserine containing peptide sequences of ovalbumin. 

 Nature, Lond. 173, 214 (1954). 



75. V. Du Vigneaud, C. Ressler, and S. Trippett: The sequence of amino acids in oxytocin, 

 with a proposal for the structure of oxytocin. /. Biol. Chem. 205, 949-957 (1953). 



76. E.O. P. Thompson: Crystalline papain. IV. Free amino groups and N-terminal sequence. 

 J. Biol. Chem. 207, 563-574 (1954). 



77. M. B. Williamson and J. M. Passman: The amino acid sequence at the N terminus of 

 pepsin. /. Biol. Chem. Ill, 151-157 (1956). 



78. D. Cole and C. H. Li: N-terminal sequence of prolactin. Fed. Proc. 14, 195 (1955). 



79. C. H. W. HiNS, W. H. Stein, and S. Moore: Peptides obtained by chymotryptic hy- 

 drolysis of performic acid-oxidized ribonuclease. A partial structural formula for the 

 oxidized protein. J. Biol. Chem. Ill, 151-169 (1956). 



80. R. Monier and M. Jutisz: Contribution a Tetude de la structure de la salmine d'Oncor- 

 hyncus. Biochim. Biophys. Acta 14, 551-558 (1954). 



81. R. Monier and M. Jutisz: Contribution a I'etude de la structure de la salmine d'On- 

 chorhynchus. II. Etude de quelques peptides resultant de I'hydrolyse trypsique. Biochim. 

 Biophys. Acta 15, 62-68 (1955). 



82. F. Lucas, J. T. B. Shaw, and S. G. Smith: Amino-acid sequence in a fraction of Bombyx 

 silk fibroin. Nature, Lond. 178, 861 (1956). 



83. L. M. Kay and W. A. Schroeder: The chromatographic separation and identification 

 of some peptides in partial hydrolysates of silk fibroin. /. Amer. Chem. Soc. 76, 3564- 

 3568 (1954). 



84. E. Abderhalden and A. Bahn: Isolierung von tyrosyl-seryl-prolyl-tyrosin beim 

 stufenweisen abbau von seidenfibroin (Bombyx Mori). Hoppe-Seyl. Z. 219, 72-81 (1933). 



85. E. W. Davie and H. Neurath: Identification of a peptide released during autocatalytic 

 activation of trypsinogen. J. Biol. Chem. Ill, 515-529 (1955). 



86. R. Consden and A. H. Gordon: A study of the peptides of cystine in partial hydro- 

 lysates of wool. Biochem. J. 46, 8-20 (1950). 



87. A. Polson: Quantitative partition chromatography and the composition of E. coli. 

 Biochim. Biophys. Acta 2, 575-581 (1948). 



88. R. B. Roberts, D. B. Cowie, P. H. Abelson, E. T. Bolton, and R. J. Britten: Studies 

 of biosynthesis in Escherichia coli. Carnegie Institution of Washington Publication 

 607, p. 28, Washington, D.C. (1955). 



89. D. Elson and E. Chargaff: Evidence of common regularities in the composition of 

 pentose nucleic acids. Biochim. Biophys. Acta 17, 367-376 (1955). 



90. F. Friedberg: The amino acid composition of adenosine triphosphate-creatine trans- 

 phosphorylase. Arch. Biochem. Biophys. 61, 263-266 (1956). 



