Ultraviolet Difference Spectra in Human Hemoglobin
نویسندگان
چکیده
منابع مشابه
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...
متن کاملStudies 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...
متن کاملUltraviolet 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...
متن کاملAcid Difference Spectra of Human Carbonic Anhydrases.
Human carbonic anhydrase B loses enzymatic activity as it undergoes an irreversible conformational change near pH 4 (1). Riddiford (2) further found that seven of the eleven histidyl groups, which are unreactive in the native protein, become titratable during this change. Also, five or six of the eight tyrosyl groups do not ionize freely and reversibly in the native protein (2, 3). Human carbon...
متن کاملUltraviolet Difference Spectra of Tyrosine Groups in Proteins and Amino Acids*t
The ultraviolet absorption of protein solutions at wave lengths greater than 2500 A is due chiefly to the aromatic side chains of tyrosine, phenylalanine, and tryptophan (1,2). When a protein is titrated with a.lkali, a ncm, stronger absorption band appears with a maximum at about 2930 A, because of the ionization of tyrosyl residues. This marked change in absorption has been used to estimate t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)63366-6