Inaccessibility of tryptophan residues of recombinant human renin to quenching agents.
The fluorescence quenching of the three tryptophan residues of recombinant human renin was determined using ionic and penetrating quenchers. Tryptophans 44,200, and 312 of recombinant human renin were found to be totally inaccessible to the ionic quenchers cesium and iodide and only partially accessible to the penetrating quencher acrylamide. The renin had a fluorescence emission maximum at 325 nm which was made up of three separate components as determined by second derivative spectroscopy. These data are in accord with solvent accessibility calculations from three-dimensional models of human renin but differ from findings published previously from similar analysis of mouse submandibular gland renin (Quay, S. C., Heropoulous, A., Commes, K., Dzau, V. J. (1985) J. Biol. Chem. 260, 15055-15058), which is 68% identical in sequence to human renin.
Epps
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Poorman
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Hui
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Carlson
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Heinrikson
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D020106:Acrylamide; D000178:Acrylamides / Q000494:pharmacology; D002586:Cesium / Q000494:pharmacology; D002712:Chlorides; D005453:Fluorescence; D006031:Glycosylation; D006801:Humans; D007454:Iodides / Q000494:pharmacology; D011487:Protein Conformation; D011489:Protein Denaturation; D011994:Recombinant Proteins; D012083:Renin; D013050:Spectrometry, Fluorescence; D014364:Tryptophan
D000178:Acrylamides; D002712:Chlorides; D007454:Iodides; D011994:Recombinant Proteins; D002586:Cesium; D020106:Acrylamide; D014364:Tryptophan; D012083:Renin; C028019:cesium chloride