Abstract:
:Phosphorescence spectroscopy on mouse myeloma IgA J539 in rigid solution at 77K revealed the type of anomalous short-lived component in the tryptophan decay originally observed with lysozyme (Churchich, J.E., 1966. Biochim. Biophys. Acta. 120:406-412) and seen in a large number of Bence Jones proteins (Longworth, J.W., C.L. McLaughlin, and A. Solomon. 1976. Biochemistry. 15:2953-2958). The decay time of the anomalous component that results from the interaction between tryptophan side chains and disulfide linkages in proteins was observed to significantly lengthen in J539 in response to binding of a galactan antigen. With hen egg-white lysozyme in which the type of fluorescence enhancement on ligand binding seen with J539 has also been observed, phosphorescence measurements revealed a similar lengthening of the decay time of the disulfide-induced anomalous component in the tryptophan decay. These perturbations are interpreted as ligand-induced changes to the tryptophan-disulfide proximities that have been shown to exist in these structures. Given the short-range nature of the disulfide perturbation (see following article) the observations suggest, in particular when combined with x-ray crystallographic data, that phosphorescence decay-time measurements of disulfide perturbations can serve as a sensitive spectroscopic indicator of subtle conformational changes in immunoglobulins and other tryptophan-disulfide containing proteins.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Li Z,Galley WCdoi
10.1016/S0006-3495(89)82681-5subject
Has Abstractpub_date
1989-08-01 00:00:00pages
353-60issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(89)82681-5journal_volume
56pub_type
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