Optical rotation and viscosity of native and denatured proteins. XIII. Further studies on enzyme proteins
The optical rotatory dispersion of aldolase, bacterial amylase, deoxyribonuclease, elastase, lactic acid dehydrogenase, lysozyme, and ribonuclease was studied by the method of spectropolarimetry. The dispersion constants (λ c ) of deoxyribonuclease and elastase were found in the same low range as th...
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Veröffentlicht in: | Archives of biochemistry and biophysics 1961-02, Vol.92 (2), p.216-220 |
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Sprache: | eng |
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Zusammenfassung: | The optical rotatory dispersion of aldolase, bacterial amylase, deoxyribonuclease, elastase, lactic acid dehydrogenase, lysozyme, and ribonuclease was studied by the method of spectropolarimetry. The dispersion constants (λ
c
) of deoxyribonuclease and elastase were found in the same low range as the constant of ribonuclease. The high dispersion constants of aldolase, lactic acid dehydrogenase, and bacterial amylase decreased strongly upon denaturation with acid, alkali, or guanidine thiocyanate. The rotatory properties of lysozyme were but little affected by alkali, although the protein could be readily denatured by guanidine thiocyanate. Complex dispersion was observed by means of ultraviolet light with lysozyme but not with ribonuclease. |
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ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/0003-9861(61)90339-3 |