ULTRAVIOLET DIFFERENCE SPECTRA OF PEPSIN

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چکیده

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Ultraviolet Difference Spectra of Pepsin

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 Angströms 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 som...

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Studies on the ultraviolet difference spectra of proteins and polypeptides.

Changes in the ultraviolet absorption spectra of proteins associated with dcnaturation or proteolysis have been intensively investigated in recent years. These studies have been, in the main, restricted to the difference spectra of proteins and model compounds in the region between 270 and 300 rnp. The changes in this region have been assigned almost entirely to the alterations in the environme...

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Ultraviolet difference spectra and the internal structure of proteins.

The absorption spectra of protein solutions in the region 250 to 310 rnp contain contributions from phenylalanine, tyrosine, and tryptophan residues. The band due to tyrosine is of particular interest since it is found to be displaced by 1 to 6 rnp toward longer wave lengths in solutions of native proteins relative to free tyrosine or its peptides. This has been clearly demonstrated in denatura...

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The Ultraviolet Absorption Spectrum of Pepsin

The ultraviolet absorption spectrum of Northrop's pure crystalline pepsin has been determined. The curve of calculated molecular extinction coefficients is given. There is noted a general resemblance of the absorption curve for pepsin to that for urease and tyrosine; the absorption band is maximum at 2750-2800 A.micro., minimum near 2500. A slight hump on either side of the peak of the extincti...

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Ultraviolet D I F F E R E N C E Spectra of Pepsin*,$ the Journal of General Physiology

A shift of pH of pepsin solutions from 4.6 to 1.0 gives rise to spectral displacemerits in the ultraviolet. If represented as difference spectra three peaks with maxima at 2770, 2850, and 2930 ,~mgstr~ms 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 s...

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ژورنال

عنوان ژورنال: Journal of General Physiology

سال: 1959

ISSN: 1540-7748,0022-1295

DOI: 10.1085/jgp.42.3.563