The fluorescence behavior of two tryptophans (Trp-134, Trp-213) in bovine serum albumin (BSA) and a single tryptophan (Trp-214) in human serum albumin (HSA) was examined. The maximum emission wavelength (lambda max) was 340.0 nm for both proteins. In a solution of sodium dodecyl sulfate (SDS), the lambda max of BSA abruptly shifted to 332 nm at 1 mM SDS and then reversed to 334 nm at 3 mM SDS. The lambda max of HSA gradually shifted to 330 nm below 3 mM SDS, although it returned to 338 nm at 10 mM SDS. In contrast to this, in a solution of dodecltrimethylammonium bromide, the lambda max positions of BSA and HSA gradually shifted to 334.0 and 331.5 nm, respectively. Differences in the fluorescence behavior of the proteins are attributed to the fact that Trp-134 exists only in BSA, with the assumption that Trp-213 of BSA behaves the same as Trp-214 of HSA. The Trp-134 behavior appears to relate to the disruption of the helical structure in the SDS solution.
Results Elevation of serum alanine aminotransferase (ALT) was found in 13 out of 25 (52%), all of whom were categorized as AN. In 13 AN patients with elevated ALT, the median of serum ALT values was 92 [39-438] IU/L. The body mass index (BMI) was significantly lower (13.5 vs. 17.3, p=0.011), and the duration since the onset of AN was shorter (4.2 years vs. 8.9 years, p=0.037) in patients with elevated ALT. The age was younger in patients with elevated ALT, even though not significant (24.5 vs. 29.8, p=0.139). Logistic regression analysis revealed that only BMI was a significant determinant for the development of hepatocellular injuries (OR=3.46; p=0.041
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