A shift of pH of pepsin solutions from 4.6 to 1.0 gives rise to spectral displacements in the ultraviolet. If represented as difference spectra three peaks with maxima at 2770, 2850, and 2930 Ångströms are present which can be attributed to the tyrosine and tryptophan residues in the protein. On mild autolysis of pepsin at pH 2.0 the absorbancy in the ultraviolet further decreases. Although some of these effects can be ascribed to the occurrence of hydrogen bonding between the aromatic residues and a carboxylate ion, those observed on autolysis are caused by charge effects of newly formed polar groups in the vicinity of a chromophore. No direct relation between the optical properties described here and enzymic activity of pepsin has been observed.
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20 January 1959
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January 20 1959
ULTRAVIOLET DIFFERENCE SPECTRA OF PEPSIN
Olga O. Blumenfeld,
Olga O. Blumenfeld
From The Rockefeller Institute
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Gertrude E. Perlmann
Gertrude E. Perlmann
From The Rockefeller Institute
Search for other works by this author on:
Olga O. Blumenfeld
From The Rockefeller Institute
Gertrude E. Perlmann
From The Rockefeller Institute
Received:
June 25 1958
Online ISSN: 1540-7748
Print ISSN: 0022-1295
Copyright, 1959, by The Rockefeller Institute
1959
J Gen Physiol (1959) 42 (3): 563–570.
Article history
Received:
June 25 1958
Citation
Olga O. Blumenfeld, Gertrude E. Perlmann; ULTRAVIOLET DIFFERENCE SPECTRA OF PEPSIN . J Gen Physiol 20 January 1959; 42 (3): 563–570. doi: https://doi.org/10.1085/jgp.42.3.563
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