Covalent structure of bovine trypsinogen. The position of the remaining amides.

Our recent paper concerning bovine trypsinogen1,2 presented a description of the primary structure of this protein, including the disulfide bridges. However, at that time an unequivocal assignment of all amino acid residues had not been made for several amino acid residues (positions 121, 177, 180). Thus it was not known whether these residues occurred in the form of acids or amides. The aspartic acid residue in position 151 has now been correctly determined as asparagine. The aim of the present communication was to remove all these uncertainties and to complete the investigation of the covalent structure of this protein. A preliminary report of this work was presented at the Third Federation Meeting of European Biochemical Societies3.

[1]  H. Neurath,et al.  AMINO ACID SEQUENCE IN THE REGION OF DIISOPROPYL PHOSPHORYL BINDING IN DIP-TRYPSIN , 1958 .

[2]  Gray Wr,et al.  THE STRUCTURE OF A CHYMOTRYPTIC PEPTIDE FROM PSEUDOMONAS CYTOCHROME C-551. , 1963 .

[3]  Z. Deyl,et al.  Thin layer chromatography of Dansyl amino acid derivatives. , 1965, Journal of chromatography.

[4]  B. Witkop,et al.  The action of N-bromosuccinimide on trypsinogen and its derivatives. , 1960, Biochimica et biophysica acta.

[5]  P. Edman,et al.  Note on the Stepwise Degradation of Peptides via Phenyl Thiohydantoins. , 1953 .

[6]  F. Šorm,et al.  Wachstumsstimulatoren mit peptidcharakter III. Isolierung eines wachstumfaktors mit peptidcharakter aus dem enzymatischen caseinhydrolysat , 1959 .

[7]  O. Mikeš Über eiweisstoffe XXXVII. Absteigende papierelektrophorese von eiweisshydrolysaten und peptiden , 1957 .

[8]  P. Edman,et al.  A method for the determination of amino acid sequence in peptides. , 1949, Archives of biochemistry.

[9]  F. Šorm,et al.  Covalent structure of bovine trypsinogen. , 1966, Biochimica et biophysica acta.

[10]  H. Neurath,et al.  Amino acid sequence in the region of diisopropylphosphoryl binding in diisopropylphosphoryl-trypsin. , 1958, The Journal of biological chemistry.

[11]  F. Šorm,et al.  Studies on the active site of trypsin. II. The role of the imidazole ring of histidine in the catalytic action of trypsin. , 1965, Biochemical and biophysical research communications.

[12]  B. Hartley,et al.  Evolutionary Similarities between Pancreatic Proteolytic Enzymes , 1965, Nature.

[13]  V. Holeysovsky,et al.  Differentiation of dimethylaminonaphthalenesulphonic derivatives (DNS) of valine, leucine and isoleucine by chromatography on a thin layer of silica gel. , 1966, Journal of chromatography.

[14]  R. W. Drisko,et al.  Phosphopeptides from acid-hydrolyzed P32-labeled isopropyl methylphosphonofluoridate-inactivated trypsin. , 1958, The Journal of biological chemistry.