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PHOTOCHEMISTRY OF PROTEINS XXIII. PROTEIN‐PROTElN INTERACTION BETWEEN TRYPSIN, SOYBEAN TRYPSIN INHIBITOR, AND OTHER PROTEINS
Author(s) -
Estermann E. F.,
McLaren A. D.
Publication year - 1962
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1962.tb08083.x
Subject(s) - trypsin , chemistry , trypsin inhibitor , molecule , kunitz sti protease inhibitor , biochemistry , acetylation , complex formation , stereochemistry , enzyme , organic chemistry , inorganic chemistry , gene
Summary Compound formation between trypsin and inhibitor and derivatives of these proteins has been studied by means of light scattering and differential spectrophotometry. it has been fouiid that a non‐specific attraction between oppositely charged molecules is not sufficient for compound formation and that the makeup of the bonding configuration of functional groups involved in compound formation is not constant over a wide range of pH. Acetylation of the proteins does not greatly influence compound formation between trypsin and inhibitor but treatment of trypsin with DFP or ultraviolet light prevents combination.