Optical Rotatory and Ultraviolet Spectral Properties of Bence-Jones Proteins*
- 1 December 1964
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 56 (6) , 512-521
- https://doi.org/10.1093/oxfordjournals.jbchem.a128029
Abstract
In the present study, the optical rotatory and ultraviolet spectral properties of Bence-Jones proteins have been studied in relation to the antigenic type. The optical rotatory properties of native Bence-Jones proteins can not be related with the antigenic type. However, the variation of the parameter, b0 and a0, in the Moffitt-Yang equation with the solvent composition in 2-chloroethanol-water mixtures has made it possible to classify the proteins into two types. The ratio of the value of ΔOD at a peak around 293 mμ to that around 285 mμ in the difference spectra of Bence-Jones proteins caused by guanidine hydrochloride or urea is quite different depending on the antigenic type. On the basis of this fact, we have proposed a simple, spectrophotometric method to identify the type of Bencc-Jones protein. A possible structure of Bence-Jones proteins has been discussed.Keywords
This publication has 2 references indexed in Scilit:
- Structure of Muramidase (Lysozyme)The Journal of Biochemistry, 1964
- Structure of Muramidase (Lysozyme)The Journal of Biochemistry, 1964