Epidermal growth factor: internal duplication and probable relationship to pancreatic secretory trypsin inhibitor.

Abstract The sequence of the first half of epidermal growth factor is related to that of the second half, indicating a gene elongation through duplication; it is also similar to that of pancreatic secretory trypsin inhibitor, which suggests a common evolutionary origin for these two proteins. Statistical evaluation shows that it is very unlikely that either similarity in sequence could have occurred by chance. The two proteins may also be functionally related, as each forms a complex with an arginine esterase.

[1]  O. Guy,et al.  The structure of the bovine pancreatic secretory trypsin inhibitor--Kazal's inhibitor. 3. Determination of the disulfide bonds and proteolysis by thermolysin. , 1971, The Journal of biological chemistry.

[2]  S. Cohen Epidermal growth factor. , 1972, The Journal of investigative dermatology.

[3]  S. Cohen,et al.  Epidermal growth factor. Location of disulfide bonds. , 1973, The Journal of biological chemistry.

[4]  S. Odani,et al.  Studies on soybean trypsin inhibitors. IV. Complete amino acid sequence and the anti-proteinase sites of Bowman-Birk soybean proteinase inhibitor. , 1972, Journal of Biochemistry (Tokyo).

[5]  S. Cohen,et al.  The primary structure of epidermal growth factor. , 1972, The Journal of biological chemistry.

[6]  J. Taylor,et al.  Characterization of the high molecular weight form of epidermal growth factor. , 1974, The Journal of biological chemistry.

[7]  S. B. Needleman,et al.  A general method applicable to the search for similarities in the amino acid sequence of two proteins. , 1970, Journal of molecular biology.

[8]  M. O. Dayhoff,et al.  Evolution of the Structure of Ferredoxin Based on Living Relics of Primitive Amino Acid Sequences , 1966, Science.

[9]  W. Fitch An improved method of testing for evolutionary homology. , 1966, Journal of molecular biology.

[10]  J. Taylor,et al.  Epidermal growth factor. Physical and chemical properties. , 1972, The Journal of biological chemistry.

[11]  M. O. Dayhoff,et al.  The origin of the genetic material in the abnormally long human hemoglobin and chains. , 1972, Biochemical and biophysical research communications.

[12]  R. Kretsinger Gene triplication deduced from the tertiary structure of a muscle calcium binding protein. , 1972, Nature: New biology.

[13]  J. H. Collins Homology of myosin light chains, troponin-C and parvalbumins deduced from comparison of their amino acid sequences. , 1974, Biochemical and biophysical research communications.

[14]  M. Richardson Chymotryptic inhibitor I from potatoes. The amino acid sequence of subunit A. , 1974, The Biochemical journal.

[15]  L. Greene,et al.  The structure of the bovine pancreatic scretory trypsin inhibitor--Kazal's inhibitor. II. The order of the tryptic peptides. , 1969, The Journal of biological chemistry.

[16]  H. Tschesche,et al.  Über Trypsininhibitoren, IV. Die zwei spezifischen Trypsininhibitoren des Schweinepankreas , 1969 .

[17]  J. Taylor,et al.  Characterization of the binding protein for epidermal growth factor. , 1974, The Journal of biological chemistry.

[18]  F. Stevens,et al.  Amino acid sequence of lima bean protease inhibitor component IV. 2. Isolation and sequence determination of the chymotryptic peptides and the complete amino acid sequence. , 1971, European journal of biochemistry.