Although QDs have been shown to degrade under photolytic and oxidative conditions, degradation products have not been identified/defined in vivo except for the release of component core metals such as Cd and Se.
Another depolymerase enzyme, PhaZ2, has been shown to degrade PHB intracellularly ([York et al. 2003]).
High temperatures have been shown to degrade the oxide conductivity [11].
Their blends have been shown to degrade faster than their pure counterparts (Dunn et al. [2001]).
Stresses on stem and progenitor cell pools, in the form of telomere shortening (Terc−/−) or other genome maintenance failures (ATRmKO, Ku86−/−, LIG4Y288C, XPDR722W/R722W, etc)., have been shown to degrade tissue renewal capacity and accelerate the appearance of age-related phenotypes.
Grown in axenic culture in the laboratory, the fungus mycelium has been shown to degrade (in addition to lignin and cellulose) hemicelluloses, protein, soluble carbohydrates, and purified xylan and pectin using enzymes such as polyphenol oxidases, cellulases, and catalase.
Apart from Aβ, IDE has also been shown to degrade AICD [46].
Candida albicans Saps have been shown to degrade a variety of host defense proteins such as lactoferrin and immunoglobulins [30].
HPV11 E6 does not degrade p53 [13], whereas the E6 proteins from HPV16 and HPV18 have been shown to degrade p53 [22].
This could possibly be due to a relatively short period of time passing between sample date and analysis, as MMP-9 has been shown to degrade even at low temperature [31].
To determine if this mechanism accounts for some of the action of DP, we tested the effect of adenosine deaminase (AD) (1 U/ml) which has been shown to degrade extracellular adenosine at this concentration, in the adhesion assay.
