Epidermal Growth Factor

作者: John M. Taylor , William M. Mitchell , Stanley Cohen

DOI: 10.1016/S0021-9258(19)44847-3

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摘要: Abstract The major physicochemical properties of epidermal growth factor are reported. molecular weight is estimated to be approximately 6100 by the methods sedimentation equilibrium, gel filtration, and minimum calculations from amino acid analyses. Epidermal a single chain polypeptide having an asparagine amino-terminal residue arginine carboxyl-terminal residue. It further characterized absence 3 specific residues: lysine, alanine, phenylalanine. No detectable free sulfhydryl groups, hexosamines, or neutral sugars were observed. has isoelectric point pH 4.60. ultraviolet absorption spectrum typical for proteins, with E1%1 cm at 280 nm 30.9. secondary structure, as judged circular dichroism, principally nonhelical.

参考文章(35)
Albert Light, [48] Leucine aminopeptidase (LAP) Methods in Enzymology. ,vol. 11, pp. 426- 436 ,(1967) , 10.1016/S0076-6879(67)11050-1
R.David Cole, [33] S-Aminoethylation Methods in Enzymology. ,vol. 11, pp. 315- 317 ,(1967) , 10.1016/S0076-6879(67)11035-5
J.Kenneth Hoober, Stanley Cohen, Epidermal growth factor: I. The stimulation of protein and ribonucleic acid synthesis in chick embryo epidermis Biochimica et Biophysica Acta. ,vol. 138, pp. 347- 356 ,(1967) , 10.1016/0005-2787(67)90495-9
M.A. Raftery, R. David Cole, On the Aminoethylation of Proteins Journal of Biological Chemistry. ,vol. 241, pp. 3457- 3459 ,(1966) , 10.1016/S0021-9258(18)99854-6
J. Ken McDonald, Paul X. Callahan, Benjamin B. Zeitman, Stanley Ellis, Inactivation and degradation of glucagon by dipeptidyl aminopeptidase I (cathepsin C) of rat liver. Journal of Biological Chemistry. ,vol. 244, pp. 6199- 6208 ,(1969) , 10.1016/S0021-9258(18)63525-2
W M Mitchell, J H Hash, The N,O-Diacetylmuramidase of Chalaropsis Species II. PHYSICAL PROPERTIES Journal of Biological Chemistry. ,vol. 244, pp. 17- 21 ,(1969) , 10.1016/S0021-9258(19)78183-6
Milos Stastny, Stanley Cohen, Epidermal growth factor. IV. The induction of ornithine decarboxylase. Biochimica et Biophysica Acta. ,vol. 204, pp. 578- 589 ,(1970) , 10.1016/0005-2787(70)90177-2
John T. Potts, [76b] Limited proteolysis by exopeptidases Methods in Enzymology. ,vol. 11, pp. 648- 664 ,(1967) , 10.1016/S0076-6879(67)11080-X