1998
DOI: 10.1016/s0304-4165(97)00123-2
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Protective effects of carnosine against protein modification mediated by malondialdehyde and hypochlorite

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Cited by 112 publications
(78 citation statements)
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“…Referring to the experiment of Hipkiss et al, 20) we made an assay system of protein degradation by ROS to evaluate the antioxidant activity of naturally occurring antioxidants. Egg white protein (Ovalbumin, Sigma Chemicals, St. Louis, MO) dissolved in buffered saline at a concentration of 2.5 mg/ml was used as the target protein.…”
Section: Methodsmentioning
confidence: 99%
“…Referring to the experiment of Hipkiss et al, 20) we made an assay system of protein degradation by ROS to evaluate the antioxidant activity of naturally occurring antioxidants. Egg white protein (Ovalbumin, Sigma Chemicals, St. Louis, MO) dissolved in buffered saline at a concentration of 2.5 mg/ml was used as the target protein.…”
Section: Methodsmentioning
confidence: 99%
“…The antioxidant capacity of this compound is well documented, as well as its pH buffering, osmoregulating, and metalchelating abilities (Boldyrev, 1990). A potentially useful characteristic of CARN is its ability to act as an anti-glycating agent (Boldyrev, 2002;Boldyrev, 2005;Hipkiss et al, 1998;Hipkiss & Brownson, 2000), to quench superoxide anion and hydroxide radical (Pavlov, et al 1993;Rubtsov et al, 1991) and to neutralize 4-hydroxy-nonenal (HNE) and other toxic aldehydes (Aldini et al, 2002, Liu et al, 2003. In order to study the efficiency of carnosine as geroprotector, senescence accelerated mice (SAM), which have increased levels of ROS and deficiency of antioxidant capacity, was used (Boldyrev et al, 2001;Yuneva et al, 2002).…”
Section: Endogenous Antioxidantsmentioning
confidence: 99%
“…There is much evidence, mostly obtained from model systems, suggesting that carnosine can suppress protein modification mediated by reactive oxygen species (ROS) (Kohen et al, 1988;Boldyrev 2005;Alhamdani et al, 2007aAlhamdani et al, & 2007b, reactive nitrogen species (RNS) (Calabrese et al, 2005;Fontana et al, 2002), glycating agents (Hipkiss et al, 1995;Vinson and Howard, 1996;Seidler, 2000) and deleterious aldehydes such as malondialdehyde (Hipkiss et al 1997(Hipkiss et al and 1998a(Hipkiss et al and 1998b, hydroxynonenal (Aldini et al, 2002 and, acrolein Carini et al, 2003) and methylglyoxal (MG) (Hipkiss and Chana, 1998). Carnosine also inhibited the cross-linking of MG-modified protein with normal polypeptides (Hipkiss and Chana, 1998), most likely by forming adducts with the MG-induced protein carbonyl groups (Brownson and Hipkiss, 2000).…”
Section: Carnosine and Post-synthetic Protein Modificationmentioning
confidence: 99%