Changes of amino acids composition and relative digestibility of lysozyme in the reaction with .ALPHA.-dicarbonyl compounds in aqueous system.

Kato, Harubumi; Chuyên, Nguyễn Văn; Utsunomiya, Nobuko; Okitani, Akihiro

doi:10.3177/jnsv.32.55

Cited by 20 publications

(10 citation statements)

References 19 publications

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“…From this result, digestibility of casein modified by diacetyl or hexanal decreased about 20% and 40%, respectively, after 15 days of reaction, while in the case of glucose, the digestibility of glucose-modified casein slightly increased after 5 or 7 days of reaction. This result was in accordance with our previous report (11) concerning the digestibility of lysozyme modified by a dicarbonyls in aqueous system. It seemed that casein modified by glucose at preliminary stage was more readily digested by pepsin-pancreatin than the native casein.…”

supporting

confidence: 94%

Nutritional and Physiological Effects of Casein Modified by Glucose, Diacetyl, or Hexanal

Utsunomiya

Chuyên

Kato

1990

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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supporting

confidence: 94%

Nutritional and Physiological Effects of Casein Modified by Glucose, Diacetyl, or Hexanal

Utsunomiya

Chuyên

Kato

1990

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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“…Hydrolysis of buckwheat proteins with pepsin was performed according to modified method of Kato et al [11]. Simulated gastric fluid (SGF) (total vol.…”

Section: Methodsmentioning

confidence: 99%

Allergenic potential and enzymatic resistance of buckwheat

Han

2013

Nutr Res Pract

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Buckwheat is known as a health food but is one of the major food allergens triggering potentially fatal anaphylaxis in Asia, especially in Japan and Korea. This study was conducted to investigate the characteristic of enzymatic resistance of buckwheat protein and allergenic potential. Enzymatic resistance of buckwheat protein was performed with in vitro digestibility test in simulated gastric fluid (SGF), pH 1.2, using pepsin and simulated intestinal fluid (SIF) using chymotrypsin. Reactivity of buckwheat proteins to human IgE was performed using six allergic patients sensitized to buckwheat. Buckwheat's IgE levels were measured using the Phadia UniCAP-system. Buckwheat protein, 16 kDa, still remained after 30 min treatment of pepsin on SDS-PAGE. Even though 16 kDa almost disappeared after 60 min treatment, two out of the six buckwheat patients' sera showed reactivity to hydrolysate after 60 min treatment, indicating that allergenicity still remained. In simulated intestinal fluid (SIF) using chymotrypsin, buckwheat protein, 24 kDa, showed resistance to hydrolysis with chymotrypsin on SDS-PAGE, and still had allergenicity based on the result of ELISA. Our results suggest that buckwheat proteins have strong resistance to enzyme degradation. This may be attributed in part to the allergenic potential of buckwheat. Further study should be continued regarding buckwheat allergy.

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“…The reactions proceed even at physiological concentrations of MG (14) and form fluorescent products, characteristics of which resemble those occurring in proteins in aging and diabetes (15). It has been reported that MG binds and modifies a number of proteins, including bovine serum albumin (15)(16)(17)(18), ribonuclease A (19,20), lysozyme (21), and collagen (22). MG modification of protein may be closely associated with cellular toxicity.…”

mentioning

confidence: 99%

Methylglyoxal Modification of Protein

Oya

Hattori

Mizuno

et al. 1999

Journal of Biological Chemistry

338

141

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Methylglyoxal (MG), an endogenous metabolite that increases in diabetes and is a common intermediate in the Maillard reaction (glycation), reacts with proteins and forms advanced glycation end products. In the present study, we identify a novel MG-arginine adduct and also characterize the structure of a major fluorescent adduct. In addition, we describe the immunochemical study on the MG-arginine adducts using monoclonal antibody directed to MG-modified protein. On the other hand, as an immunochemical approach to the detection of these MG adducts, we raised the monoclonal antibodies (mAb3C and mAb6B) directed to the MG-modified protein and found that they specifically recognized the major fluorescent product, argpyrimidine, as the dominant epitope. The immunohistochemical analysis of the kidneys from diabetic patients revealed the localization of argpyrimidine in intima and media of small artery walls. Furthermore, the accumulation of argpyrimidine was also observed in some arterial walls of the rat brain after middle cerebral artery occlusion followed by reperfusion. These results suggest that argpyrimidine may contribute to the progression of not only long term diabetic complications, such as nephropathy and atherosclerosis, but also the tissue injury caused by ischemia/reperfusion.Nonenzymatic glycation (Maillard reaction) is a complex series of reactions between reducing sugars and amino groups of proteins, which leads to browning, fluorescence, and crosslinking of the proteins. The reaction is initiated with the reversible formation of a Schiff's base, which undergoes a rearrangement to form a relatively stable Amadori product. The Amadori product further undergoes a series of reactions through dicarbonyl intermediates to form advanced glycation end products (AGEs) 1 (1). It has been shown that the formation of AGEs in vivo contributes to the pathophysiologies associated with aging and the long term complications of diabetes (2).A number of aldehydes and ketones, in addition to sugars, are known to form AGEs. Methylglyoxal (MG), among them, has recently received considerable attention as a mediator to form AGEs. MG is known to be formed nonenzymically by amine-catalyzed sugar fragmentation reactions (3-5) and by spontaneous decomposition of triose phosphate intermediates in glycolysis (5). It is also a product of the metabolism of acetol, an intermediate in the catabolism of both threonine (6) and the ketone body acetone (7). A recent study on the formation of AGEs in endothelial cells cultured under hyperglycemic conditions indicated that MG was the major precursor of AGEs (8). Chaplen et al. (9) have shown that high levels of MG are indeed present in cultured Chinese hamster ovary cells. In addition, increased levels of MG are also found in blood from diabetic patients and in the lens of streptozotosin-induced diabetic rats (10, 11). Che et al. (12) have reported that MG induces gene expression of heparin-binding epidermal growth factor-like growth factor by provoking oxidative stress. It is also known ...

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Changes of amino acids composition and relative digestibility of lysozyme in the reaction with .ALPHA.-dicarbonyl compounds in aqueous system.

Cited by 20 publications

References 19 publications

Nutritional and Physiological Effects of Casein Modified by Glucose, Diacetyl, or Hexanal

Nutritional and Physiological Effects of Casein Modified by Glucose, Diacetyl, or Hexanal

Allergenic potential and enzymatic resistance of buckwheat

Methylglyoxal Modification of Protein

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