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![[Figure 1]](hi5560fig1mag.jpg)
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Figure 1
Chemical check for the polypeptide cleavage of lysozyme by monochromatic irradiation. (a) SDS polyacrylamide gel analysis of lysozyme solutions with different levels of accumulated doses. (i) Molecular weight markers are: triosephosphate isomerase (26.6 kDa), myoglobin (16.9 kDa), α-lactoalbumin (14.4 kDa) and aprotinin (6.5 kDa); (ii) no exposure; (iii) 433 Gy (144 Gy s−1); (iv) 1406 Gy (141 Gy s−1); (v) 4359 Gy (145 Gy s−1); (vi) 8700 Gy (145 Gy s−1). The lysozyme concentration used in the SXSS measurements was 5 mg ml−1. (b) TOF-mass spectra of lysozyme (I) before and (II) after irradiation with 8700 Gy (145 Gy s−1). The matrix buffer was sinapic acid. (c) An example of the change in SXSS of lysozyme before and after the monochromatic irradiation. Open circles represents short-exposure lysozyme (165 Gy) while solid circles express long-exposure lysozyme (3300 Gy). An upward curvature in the small S region (solid circles) points to the presence of radiation-induced aggregates. The protein concentration was 4.9 mg ml−1. |
![[Figure 1]](hi5560fig1.jpg)
 | JOURNAL OF SYNCHROTRON RADIATION |
ISSN: 1600-5775
